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Volumn 16, Issue 5, 2006, Pages 638-643

Structure and behaviour of biomolecules from Raman optical activity

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; GLYCOPROTEIN; PEPTIDE;

EID: 33749057923     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.08.004     Document Type: Review
Times cited : (58)

References (37)
  • 1
    • 0003546549 scopus 로고    scopus 로고
    • Berova N., Nakanishi K., and Woody R.W. (Eds), Wiley-VCH
    • In: Berova N., Nakanishi K., and Woody R.W. (Eds). Circular Dichroism. Principles and Applications (2000), Wiley-VCH
    • (2000) Circular Dichroism. Principles and Applications
  • 2
    • 0003976534 scopus 로고    scopus 로고
    • Cambridge University Press. This book provides the detailed theory behind ROA and other chiroptical phenomena.
    • Barron L.D. Molecular Light Scattering and Optical Activity. edn 2 (2004), Cambridge University Press. This book provides the detailed theory behind ROA and other chiroptical phenomena.
    • (2004) Molecular Light Scattering and Optical Activity. edn 2
    • Barron, L.D.1
  • 3
    • 0013227196 scopus 로고    scopus 로고
    • Raman optical activity
    • Chalmers J.M., and Griffiths P.R. (Eds), Wiley
    • Hug W. Raman optical activity. In: Chalmers J.M., and Griffiths P.R. (Eds). Handbook of Vibrational Spectroscopy vol 1 (2002), Wiley 745-758
    • (2002) Handbook of Vibrational Spectroscopy , vol.1 , pp. 745-758
    • Hug, W.1
  • 4
    • 4444355035 scopus 로고    scopus 로고
    • Raman optical activity comes of age
    • A review of molecular physics aspects of ROA, from first prediction and observation to recent chemical and biomolecular applications.
    • Barron L.D., Hecht L., Blanch E.W., and McColl I.H. Raman optical activity comes of age. Mol Phys 102 (2004) 731-744. A review of molecular physics aspects of ROA, from first prediction and observation to recent chemical and biomolecular applications.
    • (2004) Mol Phys , vol.102 , pp. 731-744
    • Barron, L.D.1    Hecht, L.2    Blanch, E.W.3    McColl, I.H.4
  • 5
    • 0001350667 scopus 로고    scopus 로고
    • A novel high-throughput Raman spectrometer for polarization difference measurements
    • Hug W., and Hangartner G. 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
  • 6
    • 0037278154 scopus 로고    scopus 로고
    • Virtual enantiomers as the solution of optical activity's deterministic offset problem
    • This paper describes refinements to the revolutionary SCP ROA instrument design, now incorporated into the BioTools ChiralRAMAN instrument, which provides rapid routine acquisition of ROA spectra of biomolecules.
    • Hug W. Virtual enantiomers as the solution of optical activity's deterministic offset problem. Appl Spectrosc 57 (2003) 1-13. This paper describes refinements to the revolutionary SCP ROA instrument design, now incorporated into the BioTools ChiralRAMAN instrument, which provides rapid routine acquisition of ROA spectra of biomolecules.
    • (2003) Appl Spectrosc , vol.57 , pp. 1-13
    • Hug, W.1
  • 7
    • 31644443201 scopus 로고    scopus 로고
    • Raman optical activity of proteins, carbohydrates and glycoproteins
    • Zhu F., Isaacs N.W., Hecht L., Tranter G.E., and Barron L.D. Raman optical activity of proteins, carbohydrates and glycoproteins. Chirality 18 (2005) 103-115
    • (2005) Chirality , vol.18 , pp. 103-115
    • Zhu, F.1    Isaacs, N.W.2    Hecht, L.3    Tranter, G.E.4    Barron, L.D.5
  • 8
    • 26444497106 scopus 로고    scopus 로고
    • Raman optical activity: a tool for protein structure analysis
    • -1. The spectra may be used, among other things, to readily distinguish between the main classes of protein structure.
    • -1. The spectra may be used, among other things, to readily distinguish between the main classes of protein structure.
    • (2005) Structure , vol.13 , pp. 1409-1419
    • Zhu, F.1    Isaacs, N.W.2    Hecht, L.3    Barron, L.D.4
  • 9
    • 2342576780 scopus 로고    scopus 로고
    • Amino acids and small peptides as building block for proteins: comparative theoretical and spectroscopic studies
    • Jalkanen K.J., Elstner M., and Suhai S. Amino acids and small peptides as building block for proteins: comparative theoretical and spectroscopic studies. J Mol Struct THEOCHEM 675 (2004) 61-77
    • (2004) J Mol Struct THEOCHEM , vol.675 , pp. 61-77
    • Jalkanen, K.J.1    Elstner, M.2    Suhai, S.3
  • 10
    • 84962476453 scopus 로고    scopus 로고
    • Ab initio calculation of vibrational Raman optical activity
    • Pecul M., and Ruud K. Ab initio calculation of vibrational Raman optical activity. Int J Quant Chem 104 (2005) 816-829
    • (2005) Int J Quant Chem , vol.104 , pp. 816-829
    • Pecul, M.1    Ruud, K.2
  • 11
    • 33645726133 scopus 로고    scopus 로고
    • Ab initio calculation of molecular chiroptical properties
    • Crawford T.D. Ab initio calculation of molecular chiroptical properties. Theor Chem Acc 115 (2006) 227-245
    • (2006) Theor Chem Acc , vol.115 , pp. 227-245
    • Crawford, T.D.1
  • 12
    • 33646242271 scopus 로고    scopus 로고
    • Conformational flexibility of L-alanine zwitterion determines shapes of Raman and Raman optical activity spectra bands
    • This study demonstrates that it is essential to take into account dynamic factors for successful simulations of the details of experimental ROA spectra.
    • Kapitán J., Baumruk V., Kopecký Jr. V., and Bouř P. Conformational flexibility of L-alanine zwitterion determines shapes of Raman and Raman optical activity spectra bands. J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory 110 (2006) 4689-4696. This study demonstrates that it is essential to take into account dynamic factors for successful simulations of the details of experimental ROA spectra.
    • (2006) J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory , vol.110 , pp. 4689-4696
    • Kapitán, J.1    Baumruk, V.2    Kopecký Jr., V.3    Bouř, P.4
  • 13
    • 0001167142 scopus 로고    scopus 로고
    • Transfer of molecular property tensors in Cartesian coordinates: a new algorithm for simulation of vibrational spectra
    • Bouř P., Sopková J., Bednárová L., Maloň P., and Keiderling T.A. Transfer of molecular property tensors in Cartesian coordinates: a new algorithm for simulation of vibrational spectra. J Comput Chem 18 (1997) 646-659
    • (1997) J Comput Chem , vol.18 , pp. 646-659
    • Bouř, P.1    Sopková, J.2    Bednárová, L.3    Maloň, P.4    Keiderling, T.A.5
  • 14
    • 0036733783 scopus 로고    scopus 로고
    • Partial optimization of molecular geometry in normal coordinates and use as a tool for simulation of vibrational spectra
    • Bouř P., and Keiderling T.A. Partial optimization of molecular geometry in normal coordinates and use as a tool for simulation of vibrational spectra. J Chem Phys 117 (2002) 4126-4132
    • (2002) J Chem Phys , vol.117 , pp. 4126-4132
    • Bouř, P.1    Keiderling, T.A.2
  • 15
    • 33644531529 scopus 로고    scopus 로고
    • Demonstration of the ring conformation in polyproline by the Raman optical activity
    • The largest system for which ROA simulations have been performed so far, thanks to the methods developed in [13,14].
    • Kapitán J., Baumruk V., and Bouř P. Demonstration of the ring conformation in polyproline by the Raman optical activity. J Am Chem Soc 128 (2006) 2438-2443. The largest system for which ROA simulations have been performed so far, thanks to the methods developed in [13,14].
    • (2006) J Am Chem Soc , vol.128 , pp. 2438-2443
    • Kapitán, J.1    Baumruk, V.2    Bouř, P.3
  • 16
    • 0842330744 scopus 로고    scopus 로고
    • Vacuum-ultraviolet circular dichroism study of saccharides by synchrotron radiation spectrophotometry
    • Matsuo K., and Gekko K. Vacuum-ultraviolet circular dichroism study of saccharides by synchrotron radiation spectrophotometry. Carbohydr Res 339 (2004) 591-597
    • (2004) Carbohydr Res , vol.339 , pp. 591-597
    • Matsuo, K.1    Gekko, K.2
  • 17
    • 33745286782 scopus 로고    scopus 로고
    • From the gas phase to aqueous solution: vibrational spectroscopy. Raman optical activity and conformational structure of carbohydrates
    • 10.1016/j.ijms.2006.01.031. The authors demonstrate the power of experimental ROA spectra combined with ab initio simulations for determining aqueous solution structure and conformational populations of small biomolecules.
    • Macleod N.A., Johannessen C., Hecht L., Barron L.D., and Simons J.P. From the gas phase to aqueous solution: vibrational spectroscopy. Raman optical activity and conformational structure of carbohydrates. Int J Mass Spectrom (2006) 10.1016/j.ijms.2006.01.031. The authors demonstrate the power of experimental ROA spectra combined with ab initio simulations for determining aqueous solution structure and conformational populations of small biomolecules.
    • (2006) Int J Mass Spectrom
    • Macleod, N.A.1    Johannessen, C.2    Hecht, L.3    Barron, L.D.4    Simons, J.P.5
  • 18
    • 3042850001 scopus 로고    scopus 로고
    • A study of α-helix hydration in polypeptides, proteins and viruses using vibrational Raman optical activity
    • McColl I.H., Blanch E.W., Hecht L., and Barron L.D. 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
  • 19
    • 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
    • McColl I.H., Blanch E.W., Gill A.C., Rhie A.G.O., Ritchie M.A., Hecht L., Nielsen K., and Barron L.D. 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
  • 21
    • 0034827721 scopus 로고    scopus 로고
    • Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity
    • Blanch E.W., Hecht L., Day L.A., Pederson D.M., and Barron L.D. 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
  • 22
    • 0036399145 scopus 로고    scopus 로고
    • Unfolded proteins studied by Raman optical activity
    • Barron L.D., Blanch E.W., and Hecht L. 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
  • 23
    • 0029058133 scopus 로고
    • II conformation for the molecular recognition of peptides
    • II conformation for the molecular recognition of peptides. Biopolymers 37 (1995) 281-292
    • (1995) Biopolymers , vol.37 , pp. 281-292
    • Siligardi, G.1    Drake, A.F.2
  • 24
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi Z., Woody R.W., and Kallenbach N.R. 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.R.3
  • 25
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability and functions
    • Bochicchio B., and Tamburro A.M. 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
  • 26
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. 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
  • 27
    • 1542347945 scopus 로고    scopus 로고
    • The conformation of tetraalanine in water determined by polarized Raman, FT-IR and VCD spectroscopy
    • Schweitzer-Stenner R., Eker F., Griebenow K., Cao X., and Nafie L.A. The conformation of tetraalanine in water determined by polarized Raman, FT-IR and VCD spectroscopy. J Am Chem Soc 126 (2004) 2768-2776
    • (2004) J Am Chem Soc , vol.126 , pp. 2768-2776
    • Schweitzer-Stenner, R.1    Eker, F.2    Griebenow, K.3    Cao, X.4    Nafie, L.A.5
  • 28
    • 3142754280 scopus 로고    scopus 로고
    • UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations
    • Asher S.A., Mikhonin A.V., and Bykov S. UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations. J Am Chem Soc 126 (2004) 8433-8440
    • (2004) J Am Chem Soc , vol.126 , pp. 8433-8440
    • Asher, S.A.1    Mikhonin, A.V.2    Bykov, S.3
  • 29
    • 1942489291 scopus 로고    scopus 로고
    • Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides
    • This work reinforces previous polypeptide and protein ROA band assignments for the PPII helix from studies of a model PPII helical oligopeptide.
    • McColl I.H., Blanch E.W., Hecht L., Kallenbach N.R., and Barron L.D. Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides. J Am Chem Soc 126 (2004) 5076-5077. This work reinforces previous polypeptide and protein ROA band assignments for the PPII helix from studies of a model PPII helical oligopeptide.
    • (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
  • 30
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau protein: implications for fibrillogenic propensity
    • Syme C.D., Blanch E.W., Holt C., Jakes R., Goedert M., Hecht L., and Barron L.D. 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
  • 31
    • 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
    • Blanch E.W., Morozova-Roche L.A., Cochran D.A.E., Doig A.J., Hecht L., and Barron L.D. 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
  • 32
    • 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
    • Blanch E.W., Gill A.C., Rhie A.G.O., Hope J., Hecht L., Nielsen K., and Barron L.D. 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
  • 33
    • 18244407049 scopus 로고    scopus 로고
    • Polypeptide and carbohydrate structure of an intact glycoprotein from Raman optical activity
    • Information about the structure of the polypeptide and carbohydrate components of AGP is deduced from the ROA spectrum of the intact glycoprotein.
    • Zhu F., Isaacs N.W., Hecht L., and Barron L.D. Polypeptide and carbohydrate structure of an intact glycoprotein from Raman optical activity. J Am Chem Soc 127 (2005) 6142-6143. Information about the structure of the polypeptide and carbohydrate components of AGP is deduced from the ROA spectrum of the intact glycoprotein.
    • (2005) J Am Chem Soc , vol.127 , pp. 6142-6143
    • Zhu, F.1    Isaacs, N.W.2    Hecht, L.3    Barron, L.D.4
  • 34
    • 0032540672 scopus 로고    scopus 로고
    • Vibrational Raman optical activity of DNA and RNA
    • Bell A.F., Hecht L., and Barron L.D. Vibrational Raman optical activity of DNA and RNA. J Am Chem Soc 120 (1998) 5820-5821
    • (1998) J Am Chem Soc , vol.120 , pp. 5820-5821
    • Bell, A.F.1    Hecht, L.2    Barron, L.D.3
  • 35
    • 33646416198 scopus 로고    scopus 로고
    • Ashton L, Barron LD, Czarnik-Matusewicz, B, Hecht L, Hyde J, Blanch EW: Two-dimensional correlation analysis of Raman optical activity data on the α-helix-to-β-sheet transition in poly(L-lysine). Mol Phys 2006, in press. This paper reports the first study of two-dimensional ROA spectroscopy, showing that additional insight into band assignments and structural changes may be obtained.
  • 36
    • 0032065180 scopus 로고    scopus 로고
    • Experimental observation of resonance Raman optical activity
    • Vargek M., Freedman T.B., Lee E., and Nafie L.A. Experimental observation of resonance Raman optical activity. Chem Phys Lett 287 (1998) 359-364
    • (1998) Chem Phys Lett , vol.287 , pp. 359-364
    • Vargek, M.1    Freedman, T.B.2    Lee, E.3    Nafie, L.A.4
  • 37
    • 33144488379 scopus 로고    scopus 로고
    • Surface-enhanced Raman optical activity on adenine in silver colloidal solution
    • Kneipp H., Kneipp J., and Kneipp K. Surface-enhanced Raman optical activity on adenine in silver colloidal solution. Anal Chem 78 (2006) 1363-1366
    • (2006) Anal Chem , vol.78 , pp. 1363-1366
    • Kneipp, H.1    Kneipp, J.2    Kneipp, K.3


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