Temperature-induced formation of a non-native intermediate state of the All β-sheet protein CD2
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[1] M C Manning,et al. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. , 1999, Biochemistry.
[2] R. Callender,et al. An FTIR study of the complex melting behavior of α-lactalbumin , 1999 .
[3] S. Radford,et al. The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate. , 1999, Journal of molecular biology.
[4] John J. Barker,et al. Engineering an intertwined form of CD2 for stability and assembly , 1998, Nature Structural Biology.
[5] C Chothia,et al. Structural determinants in the sequences of immunoglobulin variable domain. , 1998, Journal of molecular biology.
[6] M. J. Parker,et al. Topology, sequence evolution and folding dynamics of an immunoglobulin domain , 1998, Nature Structural Biology.
[7] K. Mayo,et al. A folding pathway for βpep‐4 peptide 33mer: From unfolded monomers and β‐sheet sandwich dimers to well‐structured tetramers , 1998 .
[8] S. Radford,et al. Kinetic studies of β-sheet protein folding , 1998 .
[9] H. Jane Dyson,et al. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding , 1998, Nature Structural Biology.
[10] M. J. Parker,et al. Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures. , 1998, Biochemistry.
[11] B. Kuhlman,et al. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. , 1998, Biochemistry.
[12] M Karplus,et al. "New view" of protein folding reconciled with the old through multiple unfolding simulations. , 1997, Science.
[13] P. Maček,et al. pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence. , 1997, Biochemistry.
[14] J. Rizo,et al. Cavity formation before stable hydrogen bonding in the folding of a β-clam protein , 1997, Nature Structural Biology.
[15] M. J. Parker,et al. Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. , 1997, Biochemistry.
[16] A. Fersht,et al. Circular dichroism of denatured barstar suggests residual structure,. , 1997, Biochemistry.
[17] D. Hamada,et al. The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure. , 1997, Journal of molecular biology.
[18] M. J. Parker,et al. Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. , 1997, Biochemistry.
[19] R. Woody,et al. Calculations of the CD spectrum of bovine pancreatic ribonuclease. , 1997, Biopolymers.
[20] Lorna J. Smith,et al. Native-like secondary structure in a peptide from the α-domain of hen lysozyme , 1996 .
[21] C. Betzel,et al. Crystallization and Preliminary X-ray Analysis of a Low Density Lipoprotein from Human Plasma* , 1996, The Journal of Biological Chemistry.
[22] D. Hamada,et al. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein , 1996, Nature Structural Biology.
[23] T. Arakawa,et al. Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: acid-induced denaturation. , 1996, Biochemistry.
[24] T. Arakawa,et al. Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: thermal- and trifluoroethanol-induced denaturation at neutral pH. , 1996, Biochemistry.
[25] P. Privalov,et al. Intermediate states in protein folding. , 1996, Journal of molecular biology.
[26] O. Gursky,et al. Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[27] R. Jahn,et al. A Novel Function for the Second C2 Domain of Synaptotagmin , 1996, The Journal of Biological Chemistry.
[28] P. Privalov,et al. On the entropy of protein folding , 1996, Protein science : a publication of the Protein Society.
[29] T. Tanaka,et al. High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. , 1995, Journal of molecular biology.
[30] D Eisenberg,et al. 3D domain swapping: A mechanism for oligomer assembly , 1995, Protein science : a publication of the Protein Society.
[31] C. Pace,et al. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding , 1995, Protein science : a publication of the Protein Society.
[32] Christopher M. Dobson,et al. Following protein folding in real time using NMR spectroscopy , 1995, Nature Structural Biology.
[33] C. Dobson,et al. Conformational properties of four peptides spanning the sequence of hen lysozyme. , 1995, Journal of molecular biology.
[34] J Li,et al. Conformation and function of the N-linked glycan in the adhesion domain of human CD2 , 1995, Science.
[35] O. Ptitsyn,et al. How the molten globule became. , 1995, Trends in biochemical sciences.
[36] R L Brady,et al. One sequence, two folds: a metastable structure of CD2. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[37] B. Jonsson,et al. Folding of β-sheet proteins , 1995 .
[38] M. Kataoka,et al. Thermodynamic stability of the molten globule states of apomyoglobin. , 1995, Journal of molecular biology.
[39] C. Dobson. Finding the right fold , 1995, Nature Structural Biology.
[40] A. Fersht,et al. Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution. , 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[41] K. Nishikawa,et al. Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein Folding , 1995 .
[42] P Bork,et al. The immunoglobulin fold. Structural classification, sequence patterns and common core. , 1994, Journal of molecular biology.
[43] P. S. Kim,et al. Context is a major determinant of β-sheet propensity , 1994, Nature.
[44] M. Oobatake,et al. Thermal unfolding of tetrameric melittin: Comparison with the molten globule state of cytochrome c , 1994, Protein science : a publication of the Protein Society.
[45] A. Fersht,et al. Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. , 1994, Biochemistry.
[46] L. Regan. Protein Structure: Born to be beta , 1994, Current Biology.
[47] S. Radford,et al. Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. , 1994, Biochemistry.
[48] L Serrano,et al. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. , 1994, Biochemistry.
[49] P. S. Kim,et al. Measurement of the β-sheet-forming propensities of amino acids , 1994, Nature.
[50] C Geourjon,et al. SOPM: a self-optimized method for protein secondary structure prediction. , 1994, Protein engineering.
[51] D N Woolfson,et al. Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin. , 1993, Journal of molecular biology.
[52] P E Wright,et al. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.
[53] T. Arakawa,et al. Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric "a state". , 1993, Biochemistry.
[54] A. Fersht,et al. Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. , 1993, Biochemistry.
[55] E. Reinherz,et al. Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. , 1993, Structure.
[56] 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.
[57] Janet M. Thornton,et al. Protein fold recognition , 1993, J. Comput. Aided Mol. Des..
[58] B. Rost,et al. Prediction of protein secondary structure at better than 70% accuracy. , 1993, Journal of molecular biology.
[59] S. Khorasanizadeh,et al. Folding and stability of a tryptophan-containing mutant of ubiquitin. , 1993, Biochemistry.
[60] R. L. Baldwin,et al. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. , 1993, Biochemistry.
[61] C M Dobson,et al. Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study. , 1993, Biochemistry.
[62] H. Mantsch,et al. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. , 1993, Biochemistry.
[63] David I. Stuart,et al. Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2 , 1992, Nature.
[64] C. Dobson,et al. The folding of hen lysozyme involves partially structured intermediates and multiple pathways , 1992, Nature.
[65] W. C. Johnson,et al. Environment affects amino acid preference for secondary structure. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[66] G. Fasman,et al. Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel β‐sheet in proteins , 1992, Proteins.
[67] A. Fersht,et al. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. , 1991, Biochemistry.
[68] I. Campbell,et al. Structure of domain 1 of rat T lymphocyte CD2 antigen , 1991, Nature.
[69] T. Creighton. Characterizing intermediates in protein folding , 1991, Current Biology.
[70] P. Haris,et al. Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins , 1989 .
[71] C M Dobson,et al. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. , 1989, Biochemistry.
[72] D. W. Bolen,et al. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. , 1988, Biochemistry.
[73] P. Haris,et al. Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin. , 1988, Biochimica et biophysica acta.
[74] H. Susi,et al. Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.
[75] A. Wada,et al. ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains , 1983, FEBS letters.
[76] O. Ptitsyn,et al. α‐lactalbumin: compact state with fluctuating tertiary structure? , 1981, FEBS letters.
[77] O. Fedorov,et al. Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water , 1975, Biopolymers.
[78] P. Privalov,et al. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. , 1974, Journal of molecular biology.
[79] Jenny J. Yang,et al. Nonnative intermediate state of acid-stable β-sheet protein , 2007, Cell Biochemistry and Biophysics.
[80] R. Woody. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins , 2004, European Biophysics Journal.
[81] Y. Ye,et al. Nonnative intermediate state of acid-stable beta-sheet protein. , 2000, Cell biochemistry and biophysics.
[82] D. Naumann,et al. Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy , 2000, Nature Structural Biology.
[83] S. Radford,et al. Kinetic studies of beta-sheet protein folding. , 1998, Current opinion in structural biology.
[84] K. Mayo,et al. A folding pathway for betapep-4 peptide 33mer: from unfolded monomers and beta-sheet sandwich dimers to well-structured tetramers. , 1998, Protein science : a publication of the Protein Society.
[85] K. Dill,et al. From Levinthal to pathways to funnels , 1997, Nature Structural Biology.
[86] D Eisenberg,et al. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. , 1997, Advances in protein chemistry.
[87] J. Gibrat,et al. GOR method for predicting protein secondary structure from amino acid sequence. , 1996, Methods in enzymology.
[88] D. Hamada,et al. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. , 1996, Nature structural biology.
[89] C. Dobson,et al. Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme. , 1996, Folding & design.
[90] B. Jonsson,et al. Folding of beta-sheet proteins. , 1995, Current opinion in structural biology.
[91] P S Kim,et al. Context is a major determinant of beta-sheet propensity. , 1994, Nature.
[92] E T Adman,et al. Copper protein structures. , 1991, Advances in protein chemistry.
[93] K. Kuwajima,et al. The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.
[94] H. Susi,et al. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. , 1986, Methods in enzymology.
[95] R. Woody. Chapter 2 – Circular Dichroism of Peptides , 1985 .
[96] C. Tanford. Protein denaturation. , 1968, Advances in protein chemistry.
[97] C. Levinthal. Are there pathways for protein folding , 1968 .