What vibrations tell about proteins
暂无分享,去创建一个
[1] R. Dyer,et al. Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobin. , 1997, Biochemistry.
[2] R. Nakamoto,et al. Studies of the interactions of 2',3'-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site. , 1984, The Journal of biological chemistry.
[3] P. Tonge,et al. Forces, bond lengths, and reactivity: fundamental insight into the mechanism of enzyme catalysis. , 1992, Biochemistry.
[4] Hiromi Nomura,et al. Structural changes in the calcium pump accompanying the dissociation of calcium , 2002, Nature.
[5] T. Ackermann,et al. Infrared absorbances of protein side chains. , 1998, Analytical biochemistry.
[6] S. Venyaminov,et al. Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms , 1973, Biopolymers.
[7] S. Highsmith. Solvent accessibility of the adenosine 5'-triphosphate catalytic site of sarcoplasmic reticulum CaATPase. , 1986, Biochemistry.
[8] K. Gerwert,et al. A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: kinetics of the high-affinity calcium binding at low temperature. , 1996, Biophysical journal.
[9] J. Baenziger,et al. Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: evidence for specific protein structural changes upon desensitization. , 1993, Biochemistry.
[10] Thomas G. Spiro,et al. Resonance enhancement in the ultraviolet Raman spectra of aromatic amino acids , 1985 .
[11] M. Tasumi,et al. Effects of hydration on the structure, vibrational wavenumbers, vibrational force field and resonance raman intensities of N-methylacetamide , 1998 .
[12] W. Mäntele,et al. Conformational Changes Generated in GroEL during ATP Hydrolysis as Seen by Time-resolved Infrared Spectroscopy* , 1999, The Journal of Biological Chemistry.
[13] S. Krimm,et al. General treatment of vibrations of helical molecules and application to transition dipole coupling in amide I and amide II modes of α-helical poly(l-alanine) , 1998 .
[14] B. Hess,et al. Proline residues undergo structural changes during proton pumping in bacteriorhodopsin , 1990 .
[15] W. Mäntele,et al. Structural changes of the sarcoplasmic reticulum Ca(2+)-ATPase upon nucleotide binding studied by fourier transform infrared spectroscopy. , 2000, Biophysical journal.
[16] Klaus Gerwert,et al. Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy , 2001, Nature Structural Biology.
[17] W. Mäntele. Infrared Vibrational Spectroscopy of the Photosynthetic Reaction Center , 1993 .
[18] P. Anfinrud,et al. Time-resolved mid-infrared spectroscopy: methods and biological applications. , 1997, Current opinion in structural biology.
[19] P R Carey,et al. Raman Spectroscopy, the Sleeping Giant in Structural Biology, Awakes* , 1999, The Journal of Biological Chemistry.
[20] C. Schultz. Illuminating folding intermediates , 2000, Nature Structural Biology.
[21] S. N. Timasheff,et al. Infrared spectra and protein conformations in aqueous solutions. I. The amide I band in H2O and D2O solutions. , 1967, The Journal of biological chemistry.
[22] C. Wharton,et al. Resonance Raman and Fourier transform infrared spectroscopic studies of the acyl carbonyl group in [3-(5-methyl-2-thienyl)acryloyl]chymotrypsin: evidence for artifacts in the spectra obtained by both techniques. , 1991, Biochemistry.
[23] K. Gerwert,et al. Ras catalyzes GTP hydrolysis by shifting negative charges from gamma- to beta-phosphate as revealed by time-resolved FTIR difference spectroscopy. , 2001, Biochemistry.
[24] W. Mäntele,et al. ATP-Induced phosphorylation of the sarcoplasmic reticulum Ca2+ ATPase: molecular interpretation of infrared difference spectra. , 1998, Biophysical journal.
[25] N. Yu,et al. Laser-excited Raman spectroscopy of biomolecules. I. Native lysozyme and its constituent amino acids. , 1970, Journal of molecular biology.
[26] Douglas J. Moffatt,et al. Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped Bands , 1981 .
[27] S. Krimm,et al. Infrared amide I' band of the coiled coil. , 1996, Biochemistry.
[28] A. Barth,et al. The infrared absorption of amino acid side chains. , 2000, Progress in biophysics and molecular biology.
[29] I. Noda. Generalized Two-Dimensional Correlation Method Applicable to Infrared, Raman, and other Types of Spectroscopy , 1993 .
[30] C. Wharton,et al. Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids. , 1989, Biochemical Journal.
[31] H. Mantsch,et al. Ribonuclease A revisited: infrared spectroscopic evidence for lack of native-like secondary structures in the thermally denatured state. , 1995, Biochemistry.
[32] R. Mathies,et al. Vibrational analysis of the all-trans-retinal chromophore in light-adapted bacteriorhodopsin , 1987 .
[33] A. Maeda. Application of FTIR Spectroscopy to the Structural Study on the Function of Bacteriorhodopsin , 1995 .
[34] N. Nevskaya,et al. Infrared spectra and resonance interaction of amide‐I vibration of the parallel‐chain pleated sheet , 1976 .
[35] J. H. Wang,et al. Infrared studies on the mechanism of action of carbonic anhydrase. , 1968, The Journal of biological chemistry.
[36] O. Fedorov,et al. Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water , 1975, Biopolymers.
[37] E. Brown,et al. Conformational geometry and vibrational frequencies of nucleic acid chains , 1975, Biopolymers.
[38] Sung-Hou Kim,et al. The Mechanism of GTP Hydrolysis by Ras Probed by Fourier Transform Infrared Spectroscopy* , 2000, The Journal of Biological Chemistry.
[39] R. Mitchell,et al. Determination of protein secondary structure using factor analysis of infrared spectra. , 1990, Biochemistry.
[40] P. Haris,et al. Fourier transform infrared spectroscopic studies of calcium-binding proteins , 1991 .
[41] E. Goormaghtigh,et al. The different molar absorptivities of the secondary structure types in the amide I region: an attenuated total reflection infrared study on globular proteins. , 1996, Analytical biochemistry.
[42] R. Vogel,et al. Vibrational spectroscopy as a tool for probing protein function. , 2000, Current opinion in chemical biology.
[43] D. Naumann,et al. Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. , 1996, Biochemistry.
[44] Hajime Torii,et al. Effects of Intermolecular Hydrogen-Bonding Interactions on the Amide I Mode of N-Methylacetamide: Matrix-Isolation Infrared Studies and ab Initio Molecular Orbital Calculations , 1998 .
[45] F. Goñi,et al. Structure and dynamics of membrane proteins as studied by infrared spectroscopy. , 1999, Progress in biophysics and molecular biology.
[46] E. Goormaghtigh,et al. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. , 1994, Sub-cellular biochemistry.
[47] T. Keiderling,et al. Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy. , 2000, Analytical biochemistry.
[48] H. Khorana,et al. Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine‐185 protonates and deprotonantes during the photocycle , 1988, Proteins.
[49] R. Hochstrasser,et al. STRUCTURE OF THE AMIDE I BAND OF PEPTIDES MEASURED BY FEMTOSECOND NONLINEAR-INFRARED SPECTROSCOPY , 1998 .
[50] B. Diner,et al. Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling. , 1997, Biochemistry.
[51] D. Moss,et al. Stopped flow system for FTIR difference spectroscopy of biological macromolecules , 1999 .
[52] M. Nakasako,et al. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution , 2000, Nature.
[54] R. Buchet,et al. ATP-Binding site of annexin VI characterized by photochemical release of nucleotide and infrared difference spectroscopy. , 1999, Biochemical and biophysical research communications.
[55] J. E. Tackett. FT-IR Characterization of Metal Acetates in Aqueous Solution , 1989 .
[56] K. Gerwert,et al. Evidence for light‐induced 13‐cis, 14‐s‐cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals , 1986, The EMBO journal.
[57] B. Hess,et al. Role of aspartate-96 in proton translocation by bacteriorhodopsin. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[58] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[59] E. Goormaghtigh,et al. Monitoring structural stability of trypsin inhibitor at the submolecular level by amide-proton exchange using Fourier transform infrared spectroscopy: a test case for more general application. , 1997, Biochemistry.
[60] R. Hochstrasser,et al. The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[61] W. Mäntele,et al. Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c. , 1990, European journal of biochemistry.
[62] D. Naumann,et al. Temperature‐jump‐induced refolding of ribonuclease A: A time‐resolved FTIR spectroscopic study , 1995, FEBS letters.
[63] R. Mendelsohn,et al. 13C Isotope Labeling of Hydrophobic Peptides. Origin of the Anomalous Intensity Distribution in the Infrared Amide I Spectral Region of β-Sheet Structures , 2000 .
[64] H. Michel,et al. Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy , 1996, FEBS letters.
[65] D. Oesterhelt,et al. In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[66] M. Tanokura,et al. Infrared studies of interaction between metal ions and Ca2+‐binding proteins Marker bands for identifying the types of coordination of the side‐chain COO− groups to metal ions in pike parvalbumin (pI = 4.10) , 1994, FEBS letters.
[67] E. Goormaghtigh,et al. Monitoring of secondary and tertiary structure changes in the gastric H+/K+-ATPase by infrared spectroscopy. , 2001, European journal of biochemistry.
[68] R. Callender,et al. Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. , 1994, Annual review of biophysics and biomolecular structure.
[69] S. Venyaminov,et al. Lack of gross protein structure changes in the working cycle of (Na+, K+)-dependent adenosinetriphosphatase. Evidence from infrared and intrinsic fluorescence spectroscopy data. , 1980, European journal of biochemistry.
[70] J. Herzfeld,et al. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR-->N transition. , 1995, Biochemistry.
[71] J. Rosenbusch,et al. Secondary structure of a channel‐forming protein: porin from E. coli outer membranes. , 1985, The EMBO journal.
[72] P. Haris,et al. Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. , 1993, Analytical biochemistry.
[73] H. Vogel,et al. Comparative analysis of the amino- and carboxy-terminal domains of calmodulin by Fourier transform infrared spectroscopy , 2004, European Biophysics Journal.
[74] J. Bandekar,et al. Vibrational analysis of peptides, polypeptides, and proteins. V. Normal vibrations of β‐turns , 1980 .
[75] K. Fahmy. Binding of transducin and transducin-derived peptides to rhodopsin studies by attenuated total reflection-Fourier transform infrared difference spectroscopy. , 1998, Biophysical journal.
[76] J. Lanyi,et al. Complete identification of C = O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin. , 1994, Biochemistry.
[77] H. Mantsch,et al. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. , 1993, Biochemistry.
[78] S. Marqusee,et al. Hydrogen exchange studies of protein structure. , 1998, Current opinion in biotechnology.
[79] S. Krimm,et al. Intermolecular interaction effects in the amide I vibrations of polypeptides. , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[80] R. C. Dougherty,et al. Infrared and Nuclear Magnetic Resonance Spectroscopy of Chlorophyll , 1966 .
[81] H. Mantsch,et al. Infrared spectroscopic characterization of the structural changes connected with the E1----E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum. , 1987, The Journal of biological chemistry.
[82] C. Wharton. Infrared spectroscopy of enzyme reaction intermediates. , 2000, Natural product reports.
[83] S. Venyaminov,et al. Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α‐, β‐, and random coil conformations , 1990, Biopolymers.
[84] I. Laulicht,et al. Infrared spectra of labelled compounds , 1971 .
[85] W. Mäntele,et al. Redox-induced conformational changes in myoglobin and hemoglobin: electrochemistry and ultraviolet-visible and Fourier transform infrared difference spectroscopy at surface-modified gold electrodes in an ultra-thin-layer spectroelectrochemical cell. , 1992, Biochemistry.
[86] W. Mäntele,et al. Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase. , 1991, Biochimica et biophysica acta.
[87] A. Fink,et al. Do Parallel β-Helix Proteins Have a Unique Fourier Transform Infrared Spectrum? , 2000 .
[88] P. Haris,et al. Fourier transform infrared spectroscopic studies of Ca(2+)-binding proteins. , 1991, Biochemistry.
[89] Sanford A. Asher,et al. UV resonance Raman excitation profiles of the aromatic amino acids , 1986 .
[90] B Hess,et al. Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane. , 1985, Biochemistry.
[91] G. Maes,et al. Matrix isolation infrared spectra of the complexes between methylacetate and water or hydrochloric acid , 1983 .
[92] J. Bandekar,et al. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.
[93] J. Breton. Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers. , 2001, Biochimica et biophysica acta.
[94] I. Harada,et al. Normal coordinate analysis of the indole ring , 1986 .
[95] S. Pelletier,et al. Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[96] T. Spiro,et al. Proline signals in ultraviolet resonance Raman spectra of proteins: cis−trans isomerism in polyproline and ribonuclease A , 1987 .
[97] Bernhard Lendl,et al. Time-Resolved FT-IR Spectroscopy of Chemical Reactions in Solution by Fast Diffusion-Based Mixing in a Micromachined Flow Cell , 2001 .
[98] J. Knowles,et al. Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. , 1980, Biochemistry.
[99] W. Mäntele,et al. [87] Kinetic properties of rhodopsin and bacteriorhodopsin measured by kinetic infrared spectroscopy (KIS) , 1982 .
[100] G. Vergoten,et al. On the use of ultraviolet resonance Raman intensities to elaborate molecular force fields: application to nucleic acid bases and aromatic amino acid residues models. , 1998, Biospectroscopy.
[101] P. Dhamelincourt,et al. Polarized Micro-Raman and FT-IR Spectra of L-Glutamine , 1993 .
[102] H. Susi,et al. Vibrational analysis of amino acids: cysteine, serine, β-chloroalanine , 1983 .
[103] M. Tasumi,et al. Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di‐ and tripeptides and considerations on the conformation of the extended helix , 1998 .
[104] A. Barth. Fine-structure enhancement--assessment of a simple method to resolve overlapping bands in spectra. , 2000, Spectrochimica Acta Part A - Molecular and Biomolecular Spectroscopy.
[105] T. Earnest,et al. Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[106] P. Tonge,et al. UNLOCKING THE SECRETS OF ENZYME POWER USING RAMAN SPECTROSCOPY , 1995 .
[107] D. Naumann,et al. Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study. , 1993, Journal of molecular biology.
[108] A. Barth. Phosphoenzyme conversion of the sarcoplasmic reticulum Ca(2+)-ATPase. Molecular interpretation of infrared difference spectra. , 1999, The Journal of biological chemistry.
[109] Andrei K. Dioumaev,et al. Modeling Vibrational Spectra of Amino Acid Side Chains in Proteins: The Carbonyl Stretch Frequency of Buried Carboxylic Residues , 1995 .
[110] Eric J. Simon,et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide , 1995, Nature Structural Biology.
[111] H. Vogel,et al. Isotope-edited Fourier transform infrared spectroscopy studies of calmodulin's interaction with its target peptides. , 1994, Biochemistry.
[112] E. Blout,et al. The conformation fo poly‐L‐alanine in hexafluoroisopropanol , 1972, Biopolymers.
[113] W. Krueger,et al. An infrared and circular dichroism combined approach to the analysis of protein secondary structure. , 1991, Analytical biochemistry.
[114] W. Mäntele,et al. Electrochemically induced conformational changes in cytochrome c monitored by Fourier transform infrared difference spectroscopy: influence of temperature, pH, and electrode surfaces. , 1993, Biochemistry.
[115] J. Berendzen,et al. Temperature-derivative spectroscopy: a tool for protein dynamics. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[116] M. Mizuguchi,et al. FT-IR study of the Ca2+-binding to bovine alpha-lactalbumin. Relationships between the type of coordination and characteristics of the bands due to the Asp COO- groups in the Ca2+-binding site. , 1997, FEBS letters.
[117] E Goormaghtigh,et al. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds. , 1994, Sub-cellular biochemistry.
[118] W. Caughey,et al. An infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls. , 1968, Biochemistry.
[119] R. Goody,et al. Time-resolved FTIR studies of the GTPase reaction of H-ras p21 reveal a key role for the beta-phosphate. , 1998, Biochemistry.
[120] A. Barth,et al. Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms. , 2001, Biochemistry.
[121] H. Susi,et al. Fourier Transform Infrared Study of Proteins with Parallel β-Chains. , 1987, Archives of biochemistry and biophysics.
[122] S. Krimm,et al. An infrared study of unordered poly‐L‐proline in CaCL2 solutions , 1971, Biopolymers.
[123] Richard C. Lord,et al. Introduction to Infrared and Raman Spectroscopy. , 1965 .
[124] H. Michel,et al. Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis. , 2000, Biochemistry.
[125] D. Oesterhelt,et al. Chemical reconstitution of a chloride pump inactivated by a single point mutation. , 1995, The EMBO journal.
[126] P. Tonge,et al. Direct observation of the titration of substrate carbonyl groups in the active site of alpha-chymotrypsin by resonance Raman spectroscopy. , 1989, Biochemistry.
[127] D. Czajkowsky,et al. Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change. , 1993, Biochemistry.
[128] W. Mäntele,et al. Fourier transform infrared difference spectroscopy shows no evidence for an enolization of chlorophyll a upon cation formation either in vitro or during P700 photooxidation. , 1990, Biochemistry.
[129] T. Keiderling,et al. The anomalous infrared amide I intensity distribution in (13)C isotopically labeled peptide beta-sheets comes from extended, multiple-stranded structures: an ab initio study. , 2001, Journal of the American Chemical Society.
[130] W. Mäntele,et al. Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[131] M. Pézolet,et al. Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods. , 1990, Biochemistry.
[132] M. Levitt,et al. Automatic identification of secondary structure in globular proteins. , 1977, Journal of molecular biology.
[133] R. Buchet,et al. ADP-binding and ATP-binding sites in native and proteinase-K-digested creatine kinase, probed by reaction-induced difference infrared spectroscopy. , 1997, European journal of biochemistry.
[134] N. Darnton,et al. Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[135] J. Knowles,et al. beta-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. , 1980, Biochemistry.
[136] R. Hochstrasser,et al. Two-dimensional infrared spectroscopy of peptides by phase-controlled femtosecond vibrational photon echoes. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[137] J. H. Wang,et al. Raman difference studies of GDP and GTP binding to c-Harvey ras. , 1998, Biochemistry.
[138] M. Engelhard,et al. High-resolution solid state 13C NMR of bacteriorhodopsin: characterization of [4-13C]Asp resonances. , 1992, Biochemistry.
[139] W. Mäntele,et al. Flash-induced kinetic infrared spectroscopy applied to biochemical systems , 2004, Biophysics of structure and mechanism.
[140] H. Susi,et al. Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.
[141] I. Harada,et al. Vibrational spectra and normal coordinate analysis of p-cresol and its deuterated analogs , 1988 .
[142] M. Tasumi,et al. Application of the three-dimensional doorway-state theory to analyses of the amide-I infrared bands of globular proteins , 1992 .
[143] K. Fahmy,et al. Structural determinants of active state conformation of rhodopsin: molecular biophysics approaches. , 2000, Methods in enzymology.
[144] B. Gaber,et al. Laser Raman scattering as a probe of protein structure. , 1977, Annual review of biochemistry.
[145] C. Cantor,et al. Biophysical Chemistry: Part II: Techniques for the Study of Biological Structure and Function , 1980 .
[146] K. Hasegawa,et al. Vibrational Spectra and Ab Initio DFT Calculations of 4-Methylimidazole and Its Different Protonation Forms: Infrared and Raman Markers of the Protonation State of a Histidine Side Chain , 2000 .
[147] Jack D. Dunitz,et al. Fractional bonds: relations among their lengths, strengths, and stretching force constants , 1987 .
[148] W. Caughey,et al. Oxygen infrared spectra of oxyhemoglobins and oxymyoglobins. Evidence of two major liganded O2 structures. , 1987, Biochemistry.
[149] H. Torii. Model calculations on the amide‐I infrared bands of globular proteins , 1992 .
[150] E. Goormaghtigh,et al. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. , 1999, Biochimica et biophysica acta.
[151] W. Mäntele. Infrared and Fourier-Transform Infrared Spectroscopy , 1996 .
[152] D. Naumann,et al. Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy. , 1994, Biochemistry.
[153] T. Cotton,et al. 9 – Chlorophyll Aggregation: Coordination Interactions in Chlorophyll Monomers, Dimers, and Oligomers , 1978 .
[154] P. Dutton,et al. Electrochemical and spectroscopic investigations of the cytochrome bc1 complex from Rhodobacter capsulatus. , 1999, Biochemistry.
[155] W. Mäntele,et al. Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. , 1993, Trends in biochemical sciences.
[156] W. Hübner,et al. Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods. , 1996, Analytical biochemistry.
[157] H. Mantsch,et al. The use and misuse of FTIR spectroscopy in the determination of protein structure. , 1995, Critical reviews in biochemistry and molecular biology.
[158] S. Venyaminov,et al. Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands , 1990, Biopolymers.
[159] C. Wharton,et al. A stopped-flow apparatus for infrared spectroscopy of aqueous solutions. , 1995, The Biochemical journal.
[160] F. Hartl,et al. Recombination of protein domains facilitated by co-translational folding in eukaryotes , 1997, Nature.
[161] S. Krimm,et al. Normal vibrations of crystalline polyglycine I , 1972, Biopolymers.
[162] W. Mäntele,et al. Characterization of the primary electron donor of photosystem I, P700, by electrochemistry and Fourier transform infrared (FTIR) difference spectroscopy , 1996 .
[163] E. Goormaghtigh,et al. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange. , 1994, Sub-cellular biochemistry.
[164] W. Mäntele,et al. Investigation of models for photosynthetic electron acceptors , 1990 .
[165] P. Bouř,et al. Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[166] F. Goñi,et al. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. , 1993, Progress in biophysics and molecular biology.
[167] H. Michel,et al. Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions. , 1998, Biochimica et biophysica acta.
[168] J. Zasadzinski,et al. Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy. , 1999, The journal of peptide research : official journal of the American Peptide Society.
[169] S. Lin,et al. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts regenerated with deuterated tyrosine. , 1986, Biochemistry.
[170] B. Chakrabarti,et al. Intermolecular interaction of lens crystallins: from rotationally mobile to immobile states at high protein concentrations. , 1998, Biochemical and biophysical research communications.
[171] S. N. Timasheff,et al. Infrared Spectra and Protein Conformations in Aqueous Solutions , 1967 .
[172] T. Earnest,et al. Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. , 1990, Biophysical journal.
[173] W. Mäntele. Infrared Vibrational Spectroscopy of Reaction Centers , 1995 .
[174] B. Robert. Resonance Raman Studies in Photosynthesis — Chlorophyll and Carotenoid Molecules , 1996 .
[175] K. Gerwert,et al. Molecular Reaction Mechanisms of Proteins Monitored by Time-Resolved FTIR-Spectroscopy , 1999, Biological chemistry.
[176] N. Nevskaya,et al. Infrared spectra and resonance interaction of amide‐I vibration of the antiparallel‐chain pleated sheet , 1976, Biopolymers.
[177] Jean-Marie RuysschaertS. Tertiary Conformational Changes of the Neurospora crassa Plasma Membrane H+-ATPase Monitored by HydrogedDeuterium Exchange Kinetics , 1994 .
[178] N. Kallenbach,et al. Hydrogen exchange and structural dynamics of proteins and nucleic acids , 1983, Quarterly Reviews of Biophysics.
[179] N. Yu,et al. Laser-excited Raman spectroscopy of biomolecules: II. Native ribonuclease and α-chymotrypsin☆☆☆ , 1970 .
[180] G. Vergoten,et al. Vibrational normal modes of folded prolyl-containing peptides. Application to beta turns. , 1984, European journal of biochemistry.
[181] F. Siebert. Resonance Raman and infrared difference spectroscopy of retinal proteins. , 1990, Methods in enzymology.
[182] D. M. Briercheck,et al. Modeling Vibrational Spectra of Amino Acid Side Chains in Proteins: Effects of Protonation State, Counterion, and Solvent on Arginine C−N Stretch Frequencies† , 1999 .
[183] H. Mantsch,et al. Protein secondary structure from FT-IR spectroscopy : correlation with dihedral angles from three-dimensional Ramachandran plots , 1991 .
[184] R. Callender,et al. Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes. , 1999, Methods in enzymology.
[185] J. Trewhella,et al. Calmodulin remains extended upon binding to smooth muscle caldesmon: a combined small-angle scattering and fourier transform infrared spectroscopy study. , 2000, Biochemistry.
[186] J. Heberle,et al. Infrared Difference Spectra of the Intermediates L, M, N, and O of the Bacteriorhodopsin Photoreaction Obtained by Time-Resolved Attenuated Total Reflection Spectroscopy , 1997 .
[187] T. Miyazawa. Perturbation Treatment of the Characteristic Vibrations of Polypeptide Chains in Various Configurations , 1960 .
[188] J. Antonic,et al. Isotope-Edited Infrared Spectroscopy of Helical Peptides , 1999 .
[189] K. Fahmy,et al. Transducin-dependent protonation of glutamic acid 134 in rhodopsin. , 2000, Biochemistry.
[190] Hajime Torii,et al. Correlation between the Vibrational Frequencies of the Carboxylate Group and the Types of Its Coordination to a Metal Ion: An ab Initio Molecular Orbital Study , 1996 .
[191] C. Jung. Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy , 2000, Journal of molecular recognition : JMR.
[192] M. Engelhard,et al. Aspartic acid-212 of bacteriorhodopsin is ionized in the M and N photocycle intermediates: an FTIR study on specifically 13C-labeled reconstituted purple membranes. , 1993, Biochemistry.
[193] F. Goñi,et al. Infrared spectroscopy of phosphatidylcholines in aqueous suspension. A study of the phosphate group vibrations. , 1984, Biochimica et biophysica acta.
[194] P. Caspers,et al. HYDROGEN BONDING AND PROTEIN PERTURBATION IN BETA -LACTAM ACYL-ENZYMES OF STREPTOCOCCUS PNEUMONIAE PENICILLIN-BINDING PROTEIN PBP2X , 1999 .
[195] D. Naumann,et al. New structural insights into the refolding of ribonuclease T1 as seen by time‐resolved Fourier‐transform infrared spectroscopy , 1999, Proteins.
[196] R. Callender,et al. Relationship between Bond Stretching Frequencies and Internal Bonding for [16O4]- and [18O4]Phosphates in Aqueous Solution , 1998 .
[197] J. Vanderkooi,et al. Use of IR absorption of the carboxyl group of amino acids and their metabolites to determine pKs, to study proteins, and to monitor enzymatic activity , 1997 .
[198] Paul R. Carey. Raman Spectroscopy in Enzymology: The First 25 Years , 1998 .
[199] I. Gerothanassis,et al. Solvation state of the Tyr side chain in peptides. An FT-IR and 17O NMR approach , 1992 .
[200] R. Buchet,et al. Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study. , 1996, European journal of biochemistry.
[201] W. Pohle,et al. Interpretation of the influence of hydrogen bonding on the stretching vibrations of the PO−2 moiety , 1991 .
[202] W. Mäntele,et al. Time-resolved Infrared Spectroscopy of the Ca2+-ATPase , 1996, The Journal of Biological Chemistry.
[203] H. Khorana,et al. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. , 1988, Biochemistry.
[204] H. Michel,et al. Analysis of a putative voltage-gated prokaryotic potassium channel. , 2001, European journal of biochemistry.
[205] H. Mantsch,et al. Infrared spectroscopy: a new frontier in medicine. , 1997, Biophysical chemistry.
[206] Kenneth J. Rothschild,et al. FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model , 1992, Journal of bioenergetics and biomembranes.
[207] B. Hess,et al. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[208] E. Goormaghtigh,et al. Relevance of Protein Thin Films Prepared for Attenuated Total Reflection Fourier Transform Infrared Spectroscopy: Significance of the pH , 1996 .
[209] H. Michel,et al. Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling. , 1998, Biochemistry.
[210] J. Trewhella,et al. Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of calcium and magnesium binding , 1989 .
[211] C. Wharton,et al. Hydrogen-bonding in enzyme catalysis. Fourier-transform infrared detection of ground-state electronic strain in acyl-chymotrypsins and analysis of the kinetic consequences. , 1990, The Biochemical journal.
[212] D. Naumann. FT-INFRARED AND FT-RAMAN SPECTROSCOPY IN BIOMEDICAL RESEARCH , 2001 .
[213] S. O. Smith,et al. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. , 1996, Biophysical journal.
[214] T. Keiderling,et al. Predictions of secondary structure using statistical analyses of electronic and vibrational circular dichroism and Fourier transform infrared spectra of proteins in H2O. , 1996, Journal of molecular biology.
[215] S. Krimm,et al. Transition dipole interaction in polypeptides: Ab initio calculation of transition dipole parameters , 1984 .
[216] T. Heimburg,et al. FTIR-Spectroscopy of multistranded coiled coil proteins. , 1999, Biochemistry.
[217] W. Maentele,et al. Electrochemical and Infrared‐Spectroscopic Characterization of Redox Reactions of p‐Quinones , 1993 .
[218] Y. Dupont,et al. Evaluation of H2O activity in the free or phosphorylated catalytic site of Ca2+‐ATPase , 1983, FEBS letters.
[219] H. Kaback,et al. Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channel. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[220] W. Mäntele,et al. Protein conformational changes in tetraheme cytochromes detected by FTIR spectroelectrochemistry: Desulfovibrio desulfuricans Norway 4 and Desulfovibrio gigas cytochromes c3. , 1993, Biochemistry.
[221] N. Nevskaya,et al. Infrared spectra and resonance interactions of amide‐I and II vibrations of α‐helix , 1976 .
[222] H. Mantsch,et al. Two-dimensional IR correlation spectroscopy: sequential events in the unfolding process of the lambda cro-V55C repressor protein. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[223] A. Barth,et al. Substrate binding and enzyme function investigated by infrared spectroscopy , 2000, FEBS letters.
[224] L. Choo-Smith,et al. Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study. , 1999, The Journal of biological chemistry.
[225] Y. Chirgadze,et al. Intensities and other spectral parameters of infrared amide bands of polypeptides in the α‐helical form , 1974, Biopolymers.
[226] H. Mantsch,et al. Membrane binding induces destabilization of cytochrome c structure. , 1991, Biochemistry.
[227] G. Maes,et al. Matrix-isolation IR studies on the basic interaction sites in esters and thiolesters towards proton donors , 1988 .
[228] M. Tanokura,et al. A comparative study of the binding effects of Mg2+, Ca2+, Sr2+, and Cd2+ on calmodulin by fourier‐transform infrared spectroscopy , 1995 .
[229] J. Fitter,et al. Structural Equilibrium Fluctuations in Mesophilic and Thermophilic α-Amylase , 2000 .
[230] R. Dyer,et al. Infrared Studies of Fast Events in Protein Folding , 1999 .
[231] P. Tonge,et al. FTIR studies of hydrogen bonding between α,β-unsaturated esters and alcohols , 1996 .
[232] F. Siebert,et al. Infrared spectroscopy applied to biochemical and biological problems. , 1995, Methods in enzymology.
[233] T. Leyh,et al. Vibrational structure of GDP and GTP bound to RAS: an isotope-edited FTIR study. , 2001, Biochemistry.
[234] S. Bauer,et al. Spectroscopic Studies of the Hydrogen Bond. II. The Shift of the O–H Vibrational Frequency in the Formation of the Hydrogen Bond , 1937 .
[235] S. Krimm,et al. Vibrational analysis of peptides, polypeptides, and proteins. XXXII. α‐Poly(L‐glutamic acid) , 1985 .
[236] S. Krimm,et al. Transition dipole coupling in Amide I modes of βpolypeptides , 1975 .
[237] E. Goormaghtigh,et al. Difference between the E1 and E2 conformations of gastric H+/K+-ATPase in a multilamellar lipid film system. Characterization by fluorescence and ATR-FTIR spectroscopy under a continuous buffer flow. , 2001, European journal of biochemistry.
[238] Glen B. Deacon,et al. Relationships between the carbon-oxygen stretching frequencies of carboxylato complexes and the type of carboxylate coordination , 1980 .
[239] 藤原 昌夫. Vibrational spectroscopy of chlorophylls , 1987 .
[240] A. Wittinghofer,et al. Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[241] G. Thomas,et al. Raman markers of nonaromatic side chains in an alpha-helix assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val residues of phage fd subunits. , 1999, Biochemistry.
[242] S. Venyaminov,et al. Water (H2O and D2O) molar absorptivity in the 1000-4000 cm-1 range and quantitative infrared spectroscopy of aqueous solutions. , 1997, Analytical biochemistry.
[243] P. Haris,et al. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. , 1994, Methods in molecular biology.
[244] E. Goormaghtigh,et al. Tertiary conformational changes of the Neurospora crassa plasma membrane H(+)-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach. , 1994, The Journal of biological chemistry.
[245] J. Rabolt,et al. Vibrational analysis of peptides, polypeptides, and proteins. 3. alpha-Poly(L-alanine). , 1977, Macromolecules.
[246] E. Goormaghtigh,et al. Amide-proton exchange of water-soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy. , 1997, Biochemistry.
[247] P. Roepe,et al. Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. M412 and L550 intermediates. , 1987, Biochemistry.