UV–Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 2: selected applications

[1]  Mark Okon,et al.  pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements , 2014, Journal of Biomolecular NMR.

[2]  B. Nordén,et al.  UV transition moments of tyrosine. , 2014, The journal of physical chemistry. B.

[3]  A. Narayanan,et al.  Understanding and applying tyrosine biochemical diversity. , 2014, Molecular bioSystems.

[4]  M. Vieira,et al.  Transthyretin: a multifaceted protein , 2014, Biomolecular concepts.

[5]  P. Larkin.  Infrared and Raman Spectroscopy: Principles and Spectral Interpretation , 2011 .

[6]  Q. Hua.  Insulin: a small protein with a long journey , 2010, Protein & Cell.

[7]  D. Dunstan,et al.  Tyrosine autofluorescence as a measure of bovine insulin fibrillation. , 2009, Biophysical journal.

[8]  B. Nordén,et al.  Structure of human Rad51 protein filament from molecular modeling and site-specific linear dichroism spectroscopy , 2009, Proceedings of the National Academy of Sciences.

[9]  M. Cox.  A new look at the human Rad51 protein , 2009, Proceedings of the National Academy of Sciences.

[10]  S. Hayes,et al.  UV resonance Raman spectroscopy of TTR(105-115): determination of the pKa of tyrosine. , 2009, Physical chemistry chemical physics : PCCP.

[11]  L. Peek,et al.  Probing protein structure and dynamics by second‐derivative ultraviolet absorption analysis of cation–π interactions , 2006, Protein science : a publication of the Protein Society.

[12]  Daan J.A. Crommelin,et al.  Methods for structural analysis of protein pharmaceuticals , 2005 .

[13]  Phoebe A Rice,et al.  Crystal structure of a Rad51 filament , 2004, Nature Structural &Molecular Biology.

[14]  V. Uversky,et al.  Partially folded intermediates in insulin fibrillation. , 2003, Biochemistry.

[15]  A. Woody,et al.  Individual tyrosine side-chain contributions to circular dichroism of ribonuclease. , 2003, Biopolymers.

[16]  Tom L. Blundell,et al.  Insights into DNA recombination from the structure of a RAD51–BRCA2 complex , 2002, Nature.

[17]  R. Hayashi,et al.  Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 Å resolution , 2002, Protein science : a publication of the Protein Society.

[18]  S. Yokoyama,et al.  The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. , 1999, Journal of molecular biology.

[19]  C. Betzel,et al.  Spectroscopic investigation of phenolic groups ionization in the vipoxin neurotoxic phospholipase A2: comparison with the X-ray structure in the region of the tyrosyl residues. , 1998, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[20]  P. Baumann,et al.  Role of the human RAD51 protein in homologous recombination and double-stranded-break repair. , 1998, Trends in biochemical sciences.

[21]  L. Breydo,et al.  Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy , 1997 .

[22]  D. Klenerman,et al.  Ultraviolet Resonance Raman Spectroscopic Study of the Average Environment of Tyrosine in Native and Denatured Barnase , 1997 .

[23]  John M. Walker,et al.  The Protein Protocols Handbook , 1996, Humana Press.

[24]  I Gryczynski,et al.  Fluorescence anisotropy of tyrosine using one-and two-photon excitation. , 1995, Biophysical chemistry.

[25]  B. Schrader.  Infrared and Raman Spectroscopy , 1995 .

[26]  A. Fersht,et al.  Protein folding and stability: the pathway of folding of barnase , 1993 .

[27]  B. Nordén,et al.  Structure of RecA-DNA complexes studied by combination of linear dichroism and small-angle neutron scattering measurements on flow-oriented samples. , 1992, Journal of molecular biology.

[28]  L Serrano,et al.  The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. , 1992, Journal of molecular biology.

[29]  P. Westermark,et al.  Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. , 1991, Biochemical and biophysical research communications.

[30]  D S Moss,et al.  Segmented anisotropic refinement of bovine ribonuclease A by the application of the rigid-body TLS model. , 1989, Acta crystallographica. Section A, Foundations of crystallography.

[31]  X. Y. Liu,et al.  Fluorescence polarization decay of tyrosine in lima bean trypsin inhibitor. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[32]  R. Ragone,et al.  Determination of tyrosine exposure in proteins by second-derivative spectroscopy. , 1984, Biochemistry.

[33]  R. Ragone,et al.  Simultaneous determination of tyrosine and tryptophan residues in proteins by second-derivative spectroscopy. , 1982, Analytical biochemistry.

[34]  K. Kuwajima,et al.  Application of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumin. , 1979, Biochemistry.

[35]  Govindjee,et al.  Binding of modified adenine nucleotides to isolated coupling factor from chloroplasts as measured by polarization of fluorescence. , 1977, European journal of biochemistry.

[36]  J. Horwitz,et al.  Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77 degrees K. , 1970, Journal of the American Chemical Society.

[37]  H. Edelhoch,et al.  Structural studies on polypeptide hormones. I. Fluorescence. , 1969, The Journal of biological chemistry.

[38]  M. Wilchek,et al.  TYROSINE FLUORESCENCE IN PROTEINS , 1969, Annals of the New York Academy of Sciences.

[39]  A. Glazer,et al.  An analysis of the tyrosine circular dichroism bands in ribonuclease. , 1967, Journal of the American Chemical Society.

[40]  M. J. Gorbunoff.  Exposure of tyrosine residues in protein. Reaction of cyanuric fluoride with ribonuclease, alpha-lactalbumin, and beta-lactoglobulin. , 1967, Biochemistry.

[41]  B. Vallee,et al.  Side-chain Cotton effects of ribonuclease. , 1966, Biochemistry.

[42]  T. Ooi,et al.  LOCATION OF ABNORMAL TYROSINES IN ACTIN. , 1965, Biochemistry.

[43]  H. Edelhoch,et al.  Structural transitions of soybean trypsin inhibitor. I. The native protein in water. , 1963, The Journal of biological chemistry.

[44]  J. Hermans.  Normal and abnormal tyrosine side-chains in various heme proteins. , 1962, Biochemistry.

[45]  C. Tanford,et al.  Phenolic Hydroxyl Ionization in Proteins. II. Ribonuclease1a , 1955 .

[46]  D. Shugar.  The ultraviolet absorption spectrum of ribonuclease. , 1952, The Biochemical journal.

[47]  A. Goldfarb,et al.  The ultraviolet absorption spectra of proteins. , 1951, The Journal of biological chemistry.

[48]  A. Neuberger,et al.  The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration. , 1943, The Biochemical journal.

[49]  E. Bright Wilson,et al.  The Normal Modes and Frequencies of Vibration of the Regular Plane Hexagon Model of the Benzene Molecule , 1934 .