메뉴 건너뛰기




Volumn 13, Issue 10, 2005, Pages 1409-1419

Raman optical activity: A tool for protein structure analysis

Author keywords

[No Author keywords available]

Indexed keywords

BETA CASEIN; GLYCOPROTEIN; HYDROGEN; POLYLYSINE; POLYPEPTIDE; PROLINE DERIVATIVE; SERUM ALBUMIN;

EID: 26444497106     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.07.009     Document Type: Article
Times cited : (130)

References (60)
  • 1
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • A.A. Adzhubei, and M.J.E. Sternberg Left-handed polyproline II helices commonly occur in globular proteins J. Mol. Biol. 229 1993 472 493
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 2
    • 0000392293 scopus 로고
    • Preparation of β-casein by a modified urea fractionation method
    • R. Aschaffenburg Preparation of β-casein by a modified urea fractionation method J. Dairy Res. 30 1963 259 260
    • (1963) J. Dairy Res. , vol.30 , pp. 259-260
    • Aschaffenburg, R.1
  • 3
    • 84945610060 scopus 로고
    • Rayleigh scattering of polarized photons by molecules
    • P.W. Atkins, and L.D. Barron Rayleigh scattering of polarized photons by molecules Mol. Phys. 16 1969 453 466
    • (1969) Mol. Phys. , vol.16 , pp. 453-466
    • Atkins, P.W.1    Barron, L.D.2
  • 5
    • 33846005553 scopus 로고
    • Rayleigh and Raman scattering from optically active molecules
    • L.D. Barron, and A.D. Buckingham Rayleigh and Raman scattering from optically active molecules Mol. Phys. 20 1971 1111 1119
    • (1971) Mol. Phys. , vol.20 , pp. 1111-1119
    • Barron, L.D.1    Buckingham, A.D.2
  • 6
    • 33947087531 scopus 로고
    • Raman scattering of circularly polarized light by optically active molecules
    • L.D. Barron, M.P. Bogaard, and A.D. Buckingham Raman scattering of circularly polarized light by optically active molecules J. Am. Chem. Soc. 95 1973 603 605
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 603-605
    • Barron, L.D.1    Bogaard, M.P.2    Buckingham, A.D.3
  • 7
    • 0034118337 scopus 로고    scopus 로고
    • Solution structure and dynamics of biomolecules from Raman optical activity
    • L.D. Barron, L. Hecht, E.W. Blanch, and A.F. Bell Solution structure and dynamics of biomolecules from Raman optical activity Prog. Biophys. Mol. Biol. 73 2000 1 49
    • (2000) Prog. Biophys. Mol. Biol. , vol.73 , pp. 1-49
    • Barron, L.D.1    Hecht, L.2    Blanch, E.W.3    Bell, A.F.4
  • 8
    • 0036399145 scopus 로고    scopus 로고
    • Unfolded proteins studied by Raman optical activity
    • L.D. Barron, E.W. Blanch, and L. Hecht Unfolded proteins studied by Raman optical activity Adv. Protein Chem. 62 2002 51 90
    • (2002) Adv. Protein Chem. , vol.62 , pp. 51-90
    • Barron, L.D.1    Blanch, E.W.2    Hecht, L.3
  • 10
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 11
    • 0033516702 scopus 로고    scopus 로고
    • Raman optical activity of filamentous bacteriophages: Hydration of α-helices
    • E.W. Blanch, A.F. Bell, L. Hecht, L.A. Day, and L.D. Barron Raman optical activity of filamentous bacteriophages: hydration of α-helices J. Mol. Biol. 290 1999 1 7
    • (1999) J. Mol. Biol. , vol.290 , pp. 1-7
    • Blanch, E.W.1    Bell, A.F.2    Hecht, L.3    Day, L.A.4    Barron, L.D.5
  • 12
    • 0034636977 scopus 로고    scopus 로고
    • Is polyproline II helix the killer conformation? a Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme
    • E.W. Blanch, L.A. Morozova-Roche, D.A.E. Cochran, A.J. Doig, L. Hecht, and L.D. Barron Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme J. Mol. Biol. 301 2000 553 563
    • (2000) J. Mol. Biol. , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.E.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 13
    • 0034827721 scopus 로고    scopus 로고
    • Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity
    • E.W. Blanch, L. Hecht, L.A. Day, D.M. Pederson, and L.D. Barron Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity J. Am. Chem. Soc. 123 2001 4863 4864
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4863-4864
    • Blanch, E.W.1    Hecht, L.2    Day, L.A.3    Pederson, D.M.4    Barron, L.D.5
  • 15
    • 0036135819 scopus 로고    scopus 로고
    • Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity
    • E.W. Blanch, D.J. Robinson, L. Hecht, C.D. Syme, K. Nielsen, and L.D. Barron Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity J. Gen. Virol. 83 2002 241 246
    • (2002) J. Gen. Virol. , vol.83 , pp. 241-246
    • Blanch, E.W.1    Robinson, D.J.2    Hecht, L.3    Syme, C.D.4    Nielsen, K.5    Barron, L.D.6
  • 16
    • 4644372554 scopus 로고    scopus 로고
    • Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction
    • E.W. Blanch, A.C. Gill, A.G.O. Rhie, J. Hope, L. Hecht, K. Nielsen, and L.D. Barron Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction J. Mol. Biol. 343 2004 467 476
    • (2004) J. Mol. Biol. , vol.343 , pp. 467-476
    • Blanch, E.W.1    Gill, A.C.2    Rhie, A.G.O.3    Hope, J.4    Hecht, L.5    Nielsen, K.6    Barron, L.D.7
  • 17
    • 0021062575 scopus 로고
    • Solvent-induced distortions and the curvature of α-helices
    • T. Blundell, D. Barlow, N. Borkakoti, and J. Thornton Solvent-induced distortions and the curvature of α-helices Nature 306 1983 281 283
    • (1983) Nature , vol.306 , pp. 281-283
    • Blundell, T.1    Barlow, D.2    Borkakoti, N.3    Thornton, J.4
  • 18
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability and functions
    • B. Bochicchio, and A.M. Tamburro Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability and functions Chirality 14 2002 782 792
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 20
    • 0036402323 scopus 로고    scopus 로고
    • Determinants of the polyproline II helixfrom modelling studies
    • T.P. Creamer, and M.N. Campbell Determinants of the polyproline II helixfrom modelling studies Adv. Protein Chem. 62 2002 263 282
    • (2002) Adv. Protein Chem. , vol.62 , pp. 263-282
    • Creamer, T.P.1    Campbell, M.N.2
  • 21
    • 26444463913 scopus 로고
    • Introduction to
    • John Wiley & Sons, Inc. New York
    • M. Diem Introduction to Modern Vibrational Spectroscopy 1993 John Wiley & Sons, Inc. New York
    • (1993) Modern Vibrational Spectroscopy
    • Diem, M.1
  • 23
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 25
    • 0025405114 scopus 로고
    • An analysis of modulation experiments for Raman optical activity
    • L. Hecht, and L.D. Barron An analysis of modulation experiments for Raman optical activity Appl. Spectrosc. 44 1990 483 491
    • (1990) Appl. Spectrosc. , vol.44 , pp. 483-491
    • Hecht, L.1    Barron, L.D.2
  • 26
    • 0002377857 scopus 로고
    • Vibrational Raman optical activity in backscattering
    • L. Hecht, L.D. Barron, and W. Hug Vibrational Raman optical activity in backscattering Chem. Phys. Lett. 158 1989 341 344
    • (1989) Chem. Phys. Lett. , vol.158 , pp. 341-344
    • Hecht, L.1    Barron, L.D.2    Hug, W.3
  • 27
    • 0000321448 scopus 로고    scopus 로고
    • Raman optical activity instrument for studies of biopolymer structure and dynamics
    • L. Hecht, L.D. Barron, E.W. Blanch, A.F. Bell, and L.A. Day Raman optical activity instrument for studies of biopolymer structure and dynamics J. Raman Spectrosc. 30 1999 815 825
    • (1999) J. Raman Spectrosc. , vol.30 , pp. 815-825
    • Hecht, L.1    Barron, L.D.2    Blanch, E.W.3    Bell, A.F.4    Day, L.A.5
  • 29
    • 0013227196 scopus 로고    scopus 로고
    • Raman optical activity
    • J.M. Chalmers P.R. Griffiths John Wiley & Sons, Inc. Chichester
    • W. Hug Raman optical activity J.M. Chalmers P.R. Griffiths Handbook of Vibrational Spectroscopy, Volume 1 2002 John Wiley & Sons, Inc. Chichester 745 758
    • (2002) Handbook of Vibrational Spectroscopy, Volume 1 , pp. 745-758
    • Hug, W.1
  • 30
    • 0037278154 scopus 로고    scopus 로고
    • Virtual enantiomers as the solution of optical activity's deterministic offset problem
    • W. Hug Virtual enantiomers as the solution of optical activity's deterministic offset problem Appl. Spectrosc. 57 2003 1 13
    • (2003) Appl. Spectrosc. , vol.57 , pp. 1-13
    • Hug, W.1
  • 31
    • 0001350667 scopus 로고    scopus 로고
    • A novel high-throughput Raman spectrometer for polarization difference measurements
    • W. Hug, and G. Hangartner A novel high-throughput Raman spectrometer for polarization difference measurements J. Raman Spectrosc. 30 1999 841 852
    • (1999) J. Raman Spectrosc. , vol.30 , pp. 841-852
    • Hug, W.1    Hangartner, G.2
  • 32
    • 0000042757 scopus 로고    scopus 로고
    • Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies
    • N. Berova K. Nakanishi R.W. Woody Wiley-VCH New York
    • T.A. Keiderling Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies N. Berova K. Nakanishi R.W. Woody Circular Dichroism. Principles and Applications 2000 Wiley-VCH New York 621 666
    • (2000) Circular Dichroism. Principles and Applications , pp. 621-666
    • Keiderling, T.A.1
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 34
    • 0141918780 scopus 로고    scopus 로고
    • Complementary approaches to structure determination of icosahedral viruses
    • K.K. Lee, and J.E. Johnson Complementary approaches to structure determination of icosahedral viruses Curr. Opin. Struct. Biol. 13 2003 558 569
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 558-569
    • Lee, K.K.1    Johnson, J.E.2
  • 35
    • 0004288043 scopus 로고    scopus 로고
    • John Wiley & Sons, Inc. Chichester
    • D.A. Long The Raman Effect 2002 John Wiley & Sons, Inc. Chichester
    • (2002) The Raman Effect
    • Long, D.A.1
  • 36
    • 17144395929 scopus 로고    scopus 로고
    • Structure, electronic circular dichroism and Raman optical activity in the gas phase and in solution: A computational and experimental investigation
    • N.A. Macleod, P. Butz, J.P. Simons, G.H. Grant, C.M. Baker, and G.E. Tranter Structure, electronic circular dichroism and Raman optical activity in the gas phase and in solution: a computational and experimental investigation Phys. Chem. Chem. Phys. 7 2005 1432 1440
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 1432-1440
    • MacLeod, N.A.1    Butz, P.2    Simons, J.P.3    Grant, G.H.4    Baker, C.M.5    Tranter, G.E.6
  • 37
    • 0041519431 scopus 로고    scopus 로고
    • A new perspective on β-sheet structures using vibrational Raman optical activity: From poly(L-lysine) to the prion protein
    • I.H. McColl, E.W. Blanch, A.C. Gill, A.G.O. Rhie, M.A. Ritchie, L. Hecht, K. Nielsen, and L.D. Barron A new perspective on β-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein J. Am. Chem. Soc. 125 2003 10019 10026
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10019-10026
    • McColl, I.H.1    Blanch, E.W.2    Gill, A.C.3    Rhie, A.G.O.4    Ritchie, M.A.5    Hecht, L.6    Nielsen, K.7    Barron, L.D.8
  • 38
    • 3042850001 scopus 로고    scopus 로고
    • A study of α-helix hydration in polypeptides, proteins and viruses using vibrational Raman optical activity
    • I.H. McColl, E.W. Blanch, L. Hecht, and L.D. Barron A study of α-helix hydration in polypeptides, proteins and viruses using vibrational Raman optical activity J. Am. Chem. Soc. 126 2004 8181 8188
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8181-8188
    • McColl, I.H.1    Blanch, E.W.2    Hecht, L.3    Barron, L.D.4
  • 39
    • 1942489291 scopus 로고    scopus 로고
    • Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides
    • I.H. McColl, E.W. Blanch, L. Hecht, N.R. Kallenbach, and L.D. Barron Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides J. Am. Chem. Soc. 126 2004 5076 5077
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5076-5077
    • McColl, I.H.1    Blanch, E.W.2    Hecht, L.3    Kallenbach, N.R.4    Barron, L.D.5
  • 42
    • 0041135421 scopus 로고
    • Dual circular polarization Raman optical activity
    • L.A. Nafie, and T.B. Freedman Dual circular polarization Raman optical activity Chem. Phys. Lett. 154 1989 260 266
    • (1989) Chem. Phys. Lett. , vol.154 , pp. 260-266
    • Nafie, L.A.1    Freedman, T.B.2
  • 43
    • 4744344736 scopus 로고    scopus 로고
    • Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs
    • E.N. Orlova, and H.R. Saibil Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs Curr. Opin. Struct. Biol. 14 2004 584 590
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 584-590
    • Orlova, E.N.1    Saibil, H.R.2
  • 44
    • 0036392437 scopus 로고    scopus 로고
    • Surface features of potato virus X from fiber diffraction
    • L. Parker, A. Kendall, and G. Stubbs Surface features of potato virus X from fiber diffraction Virology 300 2002 291 295
    • (2002) Virology , vol.300 , pp. 291-295
    • Parker, L.1    Kendall, A.2    Stubbs, G.3
  • 45
    • 0000847058 scopus 로고
    • Ab initio vibrational Raman and Raman optical activity spectra
    • P.L. Polavarapu Ab initio vibrational Raman and Raman optical activity spectra J. Phys. Chem. 94 1990 8106 8112
    • (1990) J. Phys. Chem. , vol.94 , pp. 8106-8112
    • Polavarapu, P.L.1
  • 47
    • 0037104805 scopus 로고    scopus 로고
    • Gauge-origin independent density-functional theory calculations of vibrational Raman optical activity
    • K. Ruud, T. Helgaker, and P. Bour Gauge-origin independent density-functional theory calculations of vibrational Raman optical activity J. Phys. Chem. A 106 2002 7448 7455
    • (2002) J. Phys. Chem. a , vol.106 , pp. 7448-7455
    • Ruud, K.1    Helgaker, T.2    Bour, P.3
  • 48
    • 0037172179 scopus 로고    scopus 로고
    • Structure analysis of dipeptides in water by exploring and utilizing the structural sensitivity of amide III by polarized visible Raman, FTIR-spectroscopy and DFT based normal coordinate analysis
    • R. Schweitzer-Stenner, F. Eker, Q. Huang, K. Griebenow, P.A. Mroz, and P.M. Kozlowski Structure analysis of dipeptides in water by exploring and utilizing the structural sensitivity of amide III by polarized visible Raman, FTIR-spectroscopy and DFT based normal coordinate analysis J. Phys. Chem. B 106 2002 4294 4304
    • (2002) J. Phys. Chem. B , vol.106 , pp. 4294-4304
    • Schweitzer-Stenner, R.1    Eker, F.2    Huang, Q.3    Griebenow, K.4    Mroz, P.A.5    Kozlowski, P.M.6
  • 49
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Z. Shi, R.W. Woody, and N. Kallenbach Is polyproline II a major backbone conformation in unfolded proteins? Adv. Protein Chem. 62 2002 163 240
    • (2002) Adv. Protein Chem. , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.3
  • 52
    • 0024413264 scopus 로고
    • Water inserted α-helical segments implicate reverse turns as folding intermediates
    • M. Sundaralingham, and Y.C. Sekharudu Water inserted α-helical segments implicate reverse turns as folding intermediates Science 244 1989 1333 1337
    • (1989) Science , vol.244 , pp. 1333-1337
    • Sundaralingham, M.1    Sekharudu, Y.C.2
  • 53
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau protein: Implications for fibrillogenic propensity
    • C.D. Syme, E.W. Blanch, C. Holt, R. Jakes, M. Goedert, L. Hecht, and L.D. Barron A Raman optical activity study of rheomorphism in caseins, synucleins and tau protein: implications for fibrillogenic propensity Eur. J. Biochem. 269 2002 148 156
    • (2002) Eur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 54
    • 0032986173 scopus 로고    scopus 로고
    • Raman spectroscopy of protein and nucleic acid assemblies
    • G.J. Thomas Raman spectroscopy of protein and nucleic acid assemblies Annu. Rev. Biophys. Biomol. Struct. 28 1999 1 27
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 1-27
    • Thomas, G.J.1
  • 55
    • 0002660213 scopus 로고
    • Peptide backbone conformation and microenvironment of protein side chains
    • A.T. Tu Peptide backbone conformation and microenvironment of protein side chains Adv. Spectrosc. 13 1986 47 112
    • (1986) Adv. Spectrosc. , vol.13 , pp. 47-112
    • Tu, A.T.1
  • 56
    • 18444419164 scopus 로고    scopus 로고
    • Raman spectroscopy of proteins: From peptides to large assemblies
    • R. Tuma Raman spectroscopy of proteins: from peptides to large assemblies J. Raman Spectrosc. 36 2005 307 319
    • (2005) J. Raman Spectrosc. , vol.36 , pp. 307-319
    • Tuma, R.1
  • 57
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • V.N. Uversky Natively unfolded proteins: a point where biology waits for physics Protein Sci. 11 2002 739 756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 58
    • 1642308690 scopus 로고    scopus 로고
    • Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs
    • B.A. Wallace, F. Wien, A.J. Miles, J.G. Lees, S.V. Hoffmann, P. Evans, G.J. Wistow, and C. Slingsby Biomedical applications of synchrotron radiation circular dichroism spectroscopy: identification of mutant proteins associated with disease and development of a reference database for fold motifs Faraday Discuss. 126 2004 237 243
    • (2004) Faraday Discuss. , vol.126 , pp. 237-243
    • Wallace, B.A.1    Wien, F.2    Miles, A.J.3    Lees, J.G.4    Hoffmann, S.V.5    Evans, P.6    Wistow, G.J.7    Slingsby, C.8
  • 59
    • 18244407049 scopus 로고    scopus 로고
    • Polypeptide and carbohydrate structure of an intact glycoprotein from Raman optical activity
    • F. Zhu, N.W. Isaacs, L. Hecht, and L.D. Barron Polypeptide and carbohydrate structure of an intact glycoprotein from Raman optical activity J. Am. Chem. Soc. 127 2005 6142 6143
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6142-6143
    • Zhu, F.1    Isaacs, N.W.2    Hecht, L.3    Barron, L.D.4
  • 60
    • 1642307768 scopus 로고    scopus 로고
    • Rarified basis sets for the calculation of optical tensors. 1. the importance of gradients on hydrogen atoms for the Raman scattering tensor
    • G. Zuber, and W. Hug Rarified basis sets for the calculation of optical tensors. 1. The importance of gradients on hydrogen atoms for the Raman scattering tensor J. Phys. Chem. A 108 2004 2108 2118
    • (2004) J. Phys. Chem. a , vol.108 , pp. 2108-2118
    • Zuber, G.1    Hug, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.