메뉴 건너뛰기




Volumn 6, Issue 5, 2002, Pages 682-688

Protein and peptide secondary structure and conformational determination with vibrational circular dichroism

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PROTEIN;

EID: 0036802313     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(02)00369-1     Document Type: Review
Times cited : (177)

References (71)
  • 2
    • 0001911969 scopus 로고    scopus 로고
    • Circular dichroism of peptides and proteins
    • K. Nakanishi, N. Berova, & R.W. Woody. New York: Wiley-VCH
    • Sreerama N., Woody R.W. Circular dichroism of peptides and proteins. Nakanishi K., Berova N., Woody R.W., Circular Dichroism Principles and Applications. edn 2:2000;601-620 Wiley-VCH, New York.
    • (2000) Circular Dichroism Principles and Applications edn 2 , pp. 601-620
    • Sreerama, N.1    Woody, R.W.2
  • 3
    • 0026599616 scopus 로고
    • Extending CD spectra of proteins to 168nm improves the analysis for secondary structures
    • Toumadje A., Alcorn S.W., Johnson W.C. Extending CD spectra of proteins to 168nm improves the analysis for secondary structures. Anal Biochem. 200:1992;321-331.
    • (1992) Anal Biochem , vol.200 , pp. 321-331
    • Toumadje, A.1    Alcorn, S.W.2    Johnson, W.C.3
  • 4
    • 0035478472 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of protein: Secondary structure, fold recognition and structural genomics
    • Wallace B.A., Jans R.W. Synchrotron radiation circular dichroism spectroscopy of protein: secondary structure, fold recognition and structural genomics. Curr Opin Chem Biol. 5:2001;567-571.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 567-571
    • Wallace, B.A.1    Jans, R.W.2
  • 5
    • 0028686252 scopus 로고
    • Comparison of IR and Raman forms of vibrational optical activity
    • Nafie L.A., Yu G.S., Qu X., Freedman T.B. Comparison of IR and Raman forms of vibrational optical activity. Faraday Discuss. 99:1994;13-34.
    • (1994) Faraday Discuss , vol.99 , pp. 13-34
    • Nafie, L.A.1    Yu, G.S.2    Qu, X.3    Freedman, T.B.4
  • 6
    • 0000042757 scopus 로고    scopus 로고
    • Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies
    • N. Berova, K. Nakanishi, & R.A. Woody. New York: Wiley-VCH
    • Keiderling T.A. Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies. Berova N., Nakanishi K., Woody R.A., Circular Dichroism: Principles and Applications. edn 2:2000;621-666 Wiley-VCH, New York. This review encompasses peptide and protein conformational applications and methods in detail, including dispersive VCD techniques. Examples of empirical and theoretical peptide applications, including isotopes, and statistical analyses of protein VCD are discussed at length, including the basic methods employed.
    • (2000) Circular Dichroism: Principles and Applications edn 2 , pp. 621-666
    • Keiderling, T.A.1
  • 7
    • 0000025621 scopus 로고    scopus 로고
    • Vibrational Raman optical activity: From fundamentals to biochemical applications
    • K. Nakanishi, N. Berova, & R.W. Woody. New York: Wiley-VCH
    • Barron L.D., Hecht L. Vibrational Raman optical activity: from fundamentals to biochemical applications. Nakanishi K., Berova N., Woody R.W., Circular Dichroism, Principles and Applications. edn 2:2000;667-701 Wiley-VCH, New York.
    • (2000) Circular Dichroism, Principles and Applications edn 2 , pp. 667-701
    • Barron, L.D.1    Hecht, L.2
  • 8
    • 0002050277 scopus 로고    scopus 로고
    • Biological and pharmaceutical applications of vibrational optical activity
    • H. Gremlich, & B. Yan. New York: Marcel Dekker
    • Nafie L: Freedman T. Biological and pharmaceutical applications of vibrational optical activity. Gremlich H., Yan B., Infrared and Raman Spectroscopy of Biological Materials. 2001;15-54 Marcel Dekker, New York.
    • (2001) Infrared and Raman Spectroscopy of Biological Materials , pp. 15-54
    • Nafie, L.1    Freedman, T.2
  • 9
    • 0042904412 scopus 로고    scopus 로고
    • Determination of the structures of chiral molecules using vibrational circular dichroism
    • J.M. Hicks. New York: Oxford University Press
    • Stephens P.J., Devlin F.J., Amouche A. Determination of the structures of chiral molecules using vibrational circular dichroism. Hicks J.M., Chirality: Physical Chemistry. ACS Symposium Series. 810:2002;18-33 Oxford University Press, New York. The authors present a compact summary of their density functional theory/GIAO method of computing VCD spectra with the magnetic field perturbation theory and apply it to the simulation of spectra for molecules ranging from methyl oxirane (a small, rigid test case) to large species such as Trogler's base and flexible cases containing rotational isomers.
    • (2002) Chirality: Physical Chemistry. ACS Symposium Series , vol.810 , pp. 18-33
    • Stephens, P.J.1    Devlin, F.J.2    Amouche, A.3
  • 10
    • 0034063201 scopus 로고    scopus 로고
    • Determination of the structure of chiral molecules using ab initio vibrational circular dichroism spectroscopy
    • Stephens P.J., Devlin F.J. Determination of the structure of chiral molecules using ab initio vibrational circular dichroism spectroscopy. Chirality. 12:2000;172-179.
    • (2000) Chirality , vol.12 , pp. 172-179
    • Stephens, P.J.1    Devlin, F.J.2
  • 11
    • 0002123159 scopus 로고    scopus 로고
    • Vibrational circular dichroism applications to conformational analysis of biomolecules
    • G.D. Fasman. New York: Plenum
    • Keiderling T.A. Vibrational circular dichroism applications to conformational analysis of biomolecules. Fasman G.D., Circular Dichroism and the Conformational Analysis of Biomolecules. 1996;555-598 Plenum, New York.
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 555-598
    • Keiderling, T.A.1
  • 13
    • 0026355426 scopus 로고
    • Reassessment of the random coil conformation: Vibrational CD study of proline oligopeptides and related polypeptides
    • Dukor R.K., Keiderling T.A. Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides. Biopolymers. 31:1991;1747-1761.
    • (1991) Biopolymers , vol.31 , pp. 1747-1761
    • Dukor, R.K.1    Keiderling, T.A.2
  • 14
    • 0029011672 scopus 로고
    • Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure
    • Pancoska P., Bitto E., Janota V., Urbanova M., Gupta V.P., Keiderling T.A. Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure. Protein Sci. 4:1995;1384-1401.
    • (1995) Protein Sci , vol.4 , pp. 1384-1401
    • Pancoska, P.1    Bitto, E.2    Janota, V.3    Urbanova, M.4    Gupta, V.P.5    Keiderling, T.A.6
  • 15
    • 0042403620 scopus 로고    scopus 로고
    • Chirality in peptide vibrations. Ab initio computational studies of length, solvation, hydrogen bond, dipole coupling and isotope effects on vibrational CD
    • J.M. Hicks. Washington, DC: American Chemical Society
    • 1-helical) peptide VCD is presented with examples containing one to seven residues, and explicit solvent effects, all computed fully ab initio. The local nature of VCD and effects of H-bonding are illustrated. Transferred parameter calculations for 17mer peptides with two isotopic labels are compared with experimental results.
    • (2002) Chirality: Physical Chemistry. ACS Symposium Series , vol.810 , pp. 50-64
    • Kubelka, J.1    Silva, R.A.G.D.2    Bour, P.3    Decatur, S.M.4    Keiderling, T.A.5
  • 16
    • 0034654070 scopus 로고    scopus 로고
    • Structure, vibrational absorption and circular dichroism spectra, and absolute configuration of Trogler's Base
    • Aamouche A., Devlin F.J., Stephens P.J. Structure, vibrational absorption and circular dichroism spectra, and absolute configuration of Trogler's Base. J Am Chem Soc. 122:2000;2346-2354.
    • (2000) J Am Chem Soc , vol.122 , pp. 2346-2354
    • Aamouche, A.1    Devlin, F.J.2    Stephens, P.J.3
  • 17
    • 0034766960 scopus 로고    scopus 로고
    • Vibrational circular dichroism of gramicidin D in vesicles and micelles
    • Zhao C.X., Polavarapu P.L. Vibrational circular dichroism of gramicidin D in vesicles and micelles. Biopolymers. 62:2001;336-340.
    • (2001) Biopolymers , vol.62 , pp. 336-340
    • Zhao, C.X.1    Polavarapu, P.L.2
  • 18
    • 0342804292 scopus 로고    scopus 로고
    • Measurements of concentration dependence and enantiomeric purity of terpene solution as a test of a new commercial VCD spectrometer
    • Urbanova M., Setnicka V., Volka K. Measurements of concentration dependence and enantiomeric purity of terpene solution as a test of a new commercial VCD spectrometer. Chirality. 12:2000;199-203.
    • (2000) Chirality , vol.12 , pp. 199-203
    • Urbanova, M.1    Setnicka, V.2    Volka, K.3
  • 19
    • 0035508358 scopus 로고    scopus 로고
    • Polarization modulation Fourier transform infrared spectroscopy with digital signal processing: Comparison of vibrational circular dichroism methods
    • Hilario J., Drapcho D., Curbelo R., Keiderling T.A. Polarization modulation Fourier transform infrared spectroscopy with digital signal processing: comparison of vibrational circular dichroism methods. Appl Spectrosc. 55:2001;1435-1447.
    • (2001) Appl Spectrosc , vol.55 , pp. 1435-1447
    • Hilario, J.1    Drapcho, D.2    Curbelo, R.3    Keiderling, T.A.4
  • 20
    • 0034317389 scopus 로고    scopus 로고
    • Dual polarization modulation: A real-time, spectral-multiplex separation of circular dichroism from linear birefringence spectral intensities
    • Nafie L.A. Dual polarization modulation: a real-time, spectral-multiplex separation of circular dichroism from linear birefringence spectral intensities. Appl Spectrosc. 54:2000;1634-1645. A theoretical description of dual polarization modulation and an experimental demonstration of its realization in a modified, commercial ChiralIR FT-VCD spectrometer are shown to control polarization artifacts by analysis of the two modulated signals.
    • (2000) Appl Spectrosc , vol.54 , pp. 1634-1645
    • Nafie, L.A.1
  • 21
    • 84875433305 scopus 로고    scopus 로고
    • Vibrational circular dichroism of biopolymers: Summary of methods and applications
    • Edited by Braiman M and Gregoriou V. New York: Marcel Dekker Publ; in press
    • Keiderling TA, Hilario J, Kubelka J: Vibrational circular dichroism of biopolymers: Summary of methods and applications. In Vibrational Spectroscopy of Polymers and Biological Systems. Edited by Braiman M and Gregoriou V. New York: Marcel Dekker Publ; in press.
    • Vibrational Spectroscopy of Polymers and Biological Systems
    • Keiderling, T.A.1    Hilario, J.2    Kubelka, J.3
  • 22
    • 0030134242 scopus 로고    scopus 로고
    • The measurement of dispersive vibrational CD: Signal optimization and artifact reduction
    • Xie P., Diem M. The measurement of dispersive vibrational CD: signal optimization and artifact reduction. Appl Spectrosc. 50:1996;675-680.
    • (1996) Appl Spectrosc , vol.50 , pp. 675-680
    • Xie, P.1    Diem, M.2
  • 23
    • 0031165583 scopus 로고    scopus 로고
    • Double polarization modulation interferometry
    • Polavarapu P.L. Double polarization modulation interferometry. Appl Spectrosc. 51:1997;770-777.
    • (1997) Appl Spectrosc , vol.51 , pp. 770-777
    • Polavarapu, P.L.1
  • 24
    • 0029790392 scopus 로고    scopus 로고
    • What is the crucial factor for vibrational crcular dichroism in hemoprotein ligands
    • Teraoka J., Yamamoto N., Matsumoto Y., Kyogoku Y., Sugeta H. What is the crucial factor for vibrational crcular dichroism in hemoprotein ligands. J Am Chem Soc. 118:1996;8875-8878.
    • (1996) J Am Chem Soc , vol.118 , pp. 8875-8878
    • Teraoka, J.1    Yamamoto, N.2    Matsumoto, Y.3    Kyogoku, Y.4    Sugeta, H.5
  • 25
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins. 35:1999;307-312.
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 26
    • 0031213772 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectra of proteins in the amide III region. Measurement and correlation of bandshape to secondary structure
    • Baello B.I., Pancoska P., Keiderling T.A. Vibrational circular dichroism spectra of proteins in the amide III region. Measurement and correlation of bandshape to secondary structure. Anal Biochem. 250:1997;212-221.
    • (1997) Anal Biochem , vol.250 , pp. 212-221
    • Baello, B.I.1    Pancoska, P.2    Keiderling, T.A.3
  • 28
    • 0034630136 scopus 로고    scopus 로고
    • Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy
    • Baello B., Pancoska P., Keiderling T.A. Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy. Anal Biochem. 280:2000;46-57.
    • (2000) Anal Biochem , vol.280 , pp. 46-57
    • Baello, B.1    Pancoska, P.2    Keiderling, T.A.3
  • 29
    • 0032686991 scopus 로고    scopus 로고
    • Novel use of a static modification of two-dimensional correlation analysis. Part I: Comparsion of the secondary structure sensitivity of electronic circular dichroism, FT-IR and Raman of proteins
    • Pancoska P., Kubelka J., Keiderling T.A. Novel use of a static modification of two-dimensional correlation analysis. Part I: comparsion of the secondary structure sensitivity of electronic circular dichroism, FT-IR and Raman of proteins. Appl Spectrosc. 53:1999;655-665.
    • (1999) Appl Spectrosc , vol.53 , pp. 655-665
    • Pancoska, P.1    Kubelka, J.2    Keiderling, T.A.3
  • 30
    • 0032648831 scopus 로고    scopus 로고
    • Novel use of a static modification of two-dimensional correlation analysis. Part II: Hetero-spectral correlations of protein Raman, FT-IR, and circular dichroism spectra
    • Kubelka J., Pancoska P., Keiderling T.A. Novel use of a static modification of two-dimensional correlation analysis. Part II: hetero-spectral correlations of protein Raman, FT-IR, and circular dichroism spectra. Appl Spectrosc. 53:1999;666-671.
    • (1999) Appl Spectrosc , vol.53 , pp. 666-671
    • Kubelka, J.1    Pancoska, P.2    Keiderling, T.A.3
  • 31
    • 0035899711 scopus 로고    scopus 로고
    • Temperature influence on the secondary structure of avidin and avidin-biotin complex: A vibrational circular dichroism study
    • Wang F., Polavarapu P.L. Temperature influence on the secondary structure of avidin and avidin-biotin complex: a vibrational circular dichroism study. J Phys Chem. 105:2001;7857-7864.
    • (2001) J Phys Chem , vol.105 , pp. 7857-7864
    • Wang, F.1    Polavarapu, P.L.2
  • 32
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-sheet strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Venyaminov S.Y., Woody R.W. Estimation of the number of α-helical and β-sheet strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8:1999;370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 33
    • 0033081266 scopus 로고    scopus 로고
    • Novel matrix descriptor for secondary structure segments in proteins: Demonstration of predictability from circular dichroism spectra
    • Pancoska P., Janota V., Keiderling T.A. Novel matrix descriptor for secondary structure segments in proteins: demonstration of predictability from circular dichroism spectra. Anal Biochem. 267:1999;72-83. Numbers of secondary structure segments and their interconnectivities are put into a matrix form which in turn is shown to be predictable from VCD, IR and ECD spectra, as originally applied in [34] . Given the ability to predict fractional secondary structure, this number information is equivalent to the average length of the segment. A simple version for ECD analysis was presented independently in [32] .
    • (1999) Anal Biochem , vol.267 , pp. 72-83
    • Pancoska, P.1    Janota, V.2    Keiderling, T.A.3
  • 34
    • 0029797088 scopus 로고    scopus 로고
    • Protein structural segments and their interconnections derived from optical spectra - Thermal unfolding of ribonuclease T1 as an example
    • Pancoska P., Fabian H., Yoder G., Baumruk V., Keiderling T.A. Protein structural segments and their interconnections derived from optical spectra - thermal unfolding of ribonuclease T1 as an example. Biochemistry. 35:1996;13094-13106.
    • (1996) Biochemistry , vol.35 , pp. 13094-13106
    • Pancoska, P.1    Fabian, H.2    Yoder, G.3    Baumruk, V.4    Keiderling, T.A.5
  • 35
    • 0034644437 scopus 로고    scopus 로고
    • Folding studies on the human chorionic gonadotropin β-subunit using optical spectroscopy of peptide fragments
    • Silva R.A.G.D., Sherman S.A., Perini F., Bedows E., Keiderling T.A. Folding studies on the human chorionic gonadotropin β-subunit using optical spectroscopy of peptide fragments. J Am Chem Soc. 122:2000;8623-8630. ECD IR and VCD spectra for the H1 and H2 hairpin loops in hCGβ are studied as a function of environmental perturbation. The H1 segment is shown to be a stable, monomeric β-hairpin. By comparison to previous H3 results a mechanism for the formation of the native structure of the three loops is proposed.
    • (2000) J Am Chem Soc , vol.122 , pp. 8623-8630
    • Silva, R.A.G.D.1    Sherman, S.A.2    Perini, F.3    Bedows, E.4    Keiderling, T.A.5
  • 36
  • 37
    • 0036400324 scopus 로고    scopus 로고
    • Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra
    • G.D. Rose. New York: Academic Press
    • Keiderling T.A., Xu Q. Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra. Rose G.D., Unfolded Proteins, Adv Prot Chem. 62:2002;111-162 Academic Press, New York. Full discussion of the characteristic VCD of denatured proteins and peptides by thermal and, where possible, chemical means. Correlation of the amide I′ bandshape with that of PLP II demonstrates the propensity to develop a local left-handed twist in an extended conformation. Variation of conditions (temperature) shows a more disordered state to arise, but to be often obscured in proteins by aggregation.
    • (2002) Unfolded Proteins, Adv Prot Chem , vol.62 , pp. 111-162
    • Keiderling, T.A.1    Xu, Q.2
  • 38
    • 0034972835 scopus 로고    scopus 로고
    • Conformational study on poly[γ-(α-phenethyl)-L-glutamate] using vibrational circular dichroism spectroscopy
    • Tanaka T., Inoue K., Kodama T., Kyogoku Y., Hayakawa T., Sugeta H. Conformational study on poly[γ-(α-phenethyl)-L-glutamate] using vibrational circular dichroism spectroscopy. Biopolymers. 62:2001;228-234.
    • (2001) Biopolymers , vol.62 , pp. 228-234
    • Tanaka, T.1    Inoue, K.2    Kodama, T.3    Kyogoku, Y.4    Hayakawa, T.5    Sugeta, H.6
  • 39
    • 0035700886 scopus 로고    scopus 로고
    • Nonconvalent interaction of peptides with porphyrins in aqueous solution: Conformation study using vibrational CD spectroscopy
    • Urbanova M., Setnicka V., Kral V., Volka K. Nonconvalent interaction of peptides with porphyrins in aqueous solution: conformation study using vibrational CD spectroscopy. Biopolymers. 60:2001;307-316.
    • (2001) Biopolymers , vol.60 , pp. 307-316
    • Urbanova, M.1    Setnicka, V.2    Kral, V.3    Volka, K.4
  • 40
    • 0022588380 scopus 로고
    • Vibrational circular dichroism of polypeptides. VI. Polytyrosine alpha-helical and random coil results
    • Yasui S.C., Keiderling T.A. Vibrational circular dichroism of polypeptides. VI. Polytyrosine alpha-helical and random coil results. Biopolymers. 25:1986;5-15.
    • (1986) Biopolymers , vol.25 , pp. 5-15
    • Yasui, S.C.1    Keiderling, T.A.2
  • 41
    • 0001477919 scopus 로고
    • Vibrational circular dichroism of polypeptides XI. Conformation of poly(L-lysine(Z)-L-lysine(Z)-L-1-pyrenylalanine) and poly(L-lysine(Z)- L-lysine(Z)-L-1-napthylalanine) in solution
    • Yasui S.C., Keiderling T.A., Sisido M. Vibrational circular dichroism of polypeptides XI. Conformation of poly(L-lysine(Z)-L-lysine(Z)-L-1-pyrenylalanine) and poly(L-lysine(Z)- L-lysine(Z)-L-1-napthylalanine) in solution. Macromolecules. 20:1987;2403-2406.
    • (1987) Macromolecules , vol.20 , pp. 2403-2406
    • Yasui, S.C.1    Keiderling, T.A.2    Sisido, M.3
  • 45
    • 84987322752 scopus 로고
    • The circular dichroism spectrum and structure of unordered polypeptides and proteins
    • Krimm S., Tiffany M.L. The circular dichroism spectrum and structure of unordered polypeptides and proteins. Isr J Chem. 12:1974;189-200.
    • (1974) Isr J Chem , vol.12 , pp. 189-200
    • Krimm, S.1    Tiffany, M.L.2
  • 46
    • 0033018671 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectroscopy of selected oligopeptide conformations
    • Keiderling T.A., Silva R.A.G.D., Yoder G., Dukor R.K. Vibrational circular dichroism spectroscopy of selected oligopeptide conformations. Bioorg Med Chem. 7:1999;133-141.
    • (1999) Bioorg Med Chem , vol.7 , pp. 133-141
    • Keiderling, T.A.1    Silva, R.A.G.D.2    Yoder, G.3    Dukor, R.K.4
  • 47
    • 0035814332 scopus 로고    scopus 로고
    • Differentiation of β-sheet-forming structures: Ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets
    • Kubelka J., Keiderling T.A. Differentiation of β-sheet-forming structures: ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets. J Am Chem Soc. 123:2001;12048-12058. Computations of IR and VCD spectra for β-sheets with 2-5 strands with and without twisting shows the 'characteristic' amide I β-sheet IR is a property of flat extended sheets, which have very weak VCD, in agreement with experiment. Twisting the sheets leads to significant VCD, as seen in proteins, but parallel or anti-parallel twisted sheets would be difficult to distinguish by IR or VCD.
    • (2001) J Am Chem Soc , vol.123 , pp. 12048-12058
    • Kubelka, J.1    Keiderling, T.A.2
  • 48
    • 0035936697 scopus 로고    scopus 로고
    • Interplay between hydrophobic cluster and loop propensity in β-hairpin formation
    • Espinosa J.F., Munoz V., Gellman S.H. Interplay between hydrophobic cluster and loop propensity in β-hairpin formation. J Mol Biol. 306:2001;397-402.
    • (2001) J Mol Biol , vol.306 , pp. 397-402
    • Espinosa, J.F.1    Munoz, V.2    Gellman, S.H.3
  • 49
    • 0035834063 scopus 로고    scopus 로고
    • Length-dependent stability and strand length limits in antiparallel β-sheet secondary structure
    • Stanger H.E., Syud F.A., Espinosa J.F., Giriat I., Muir T., Gellman S.H. Length-dependent stability and strand length limits in antiparallel β-sheet secondary structure. Proc Natl Acad Sci USA. 98:2001;12015-12020.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12015-12020
    • Stanger, H.E.1    Syud, F.A.2    Espinosa, J.F.3    Giriat, I.4    Muir, T.5    Gellman, S.H.6
  • 50
    • 0032246263 scopus 로고    scopus 로고
    • Minimal model systems for β-sheet secondary structure in proteins
    • Gellman S.H. Minimal model systems for β-sheet secondary structure in proteins. Curr Opin Chem Biol. 2:1998;717-725.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 717-725
    • Gellman, S.H.1
  • 51
    • 0034734312 scopus 로고    scopus 로고
    • Vibrational circular dichroism of (-hairpin peptides
    • Zhao C., Polavarapu P.L., Das C., Balaram P. Vibrational circular dichroism of (-hairpin peptides. J Am Chem Soc. 122:2000;8228-8231. VCD for a series of β-hairpins in non-polar solution stabilized by D-Pro-Gly turns are presented and compared with NMR ROSEY data showing long range NOEs between the strands and, for phenylalanine-containing variants, proposing an interaction geometry between aromatic side chains to explain their unusual ECD.
    • (2000) J Am Chem Soc , vol.122 , pp. 8228-8231
    • Zhao, C.1    Polavarapu, P.L.2    Das, C.3    Balaram, P.4
  • 53
    • 0028982307 scopus 로고
    • Conformational studies of β-turns in cyclic peptides by vibrational CD
    • Xie P., Zhou Q.W., Diem M. Conformational studies of β-turns in cyclic peptides by vibrational CD. J Am Chem Soc. 117:1995;9502-9508.
    • (1995) J Am Chem Soc , vol.117 , pp. 9502-9508
    • Xie, P.1    Zhou, Q.W.2    Diem, M.3
  • 54
    • 0028866655 scopus 로고
    • Conformational studies of cyclo-(-Pro-Gly-)(3) and its complexes with cations by vibrational circular dichroism
    • Xie P., Diem M. Conformational studies of cyclo-(-Pro-Gly-)(3) and its complexes with cations by vibrational circular dichroism. J Am Chem Soc. 117:1995;429-437.
    • (1995) J Am Chem Soc , vol.117 , pp. 429-437
    • Xie, P.1    Diem, M.2
  • 55
    • 0011150242 scopus 로고    scopus 로고
    • Linear response polarizability bandshape calculations of vibrational circular dichroism, vibrational absorption, and electronic circular dichroism of cyclo(Gly-Pro-Gly-d-Ala-Pro): A small cyclic pentapeptide having beta- and gamma- turns
    • Ito H. Linear response polarizability bandshape calculations of vibrational circular dichroism, vibrational absorption, and electronic circular dichroism of cyclo(Gly-Pro-Gly-d-Ala-Pro): a small cyclic pentapeptide having beta- and gamma- turns. Biospectroscopy. 2:1996;17-37.
    • (1996) Biospectroscopy , vol.2 , pp. 17-37
    • Ito, H.1
  • 57
    • 0030687509 scopus 로고    scopus 로고
    • 2 (n=1-4) using vibrational circular dichroism and Fourier transform infrared. Conformational determination and thermal unfolding
    • 2 (n=1-4) using vibrational circular dichroism and Fourier transform infrared. Conformational determination and thermal unfolding. Biochemistry. 36:1997;15123-15133.
    • (1997) Biochemistry , vol.36 , pp. 15123-15133
    • Yoder, G.1    Pancoska, P.2    Keiderling, T.A.3
  • 58
    • 0033596301 scopus 로고    scopus 로고
    • Isotope-edited FTIR spectroscopy of helical peptides
    • Decatur S.M., Antonic J. Isotope-edited FTIR spectroscopy of helical peptides. J Am Chem Soc. 121:1999;11914-11915.
    • (1999) J Am Chem Soc , vol.121 , pp. 11914-11915
    • Decatur, S.M.1    Antonic, J.2
  • 60
    • 0034682537 scopus 로고    scopus 로고
    • Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution
    • 13C labels in each were used to determine that while overall α-helical, the C terminus was unwound. VCD analysis showed the terminal residues to be less stable than the central ones, confirming the mechanism of unwinding from the ends with an intermediate formed between helix and coil states proposed earlier [57] .
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8318-8323
    • Silva, R.A.G.D.1    Kubelka, J.2    Decatur, S.M.3    Bour, P.4    Keiderling, T.A.5
  • 61
    • 0030874298 scopus 로고    scopus 로고
    • Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides
    • Rohl C.A., Baldwin R.L. Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides. Biochemistry. 36:1997;8435-8442.
    • (1997) Biochemistry , vol.36 , pp. 8435-8442
    • Rohl, C.A.1    Baldwin, R.L.2
  • 62
    • 0033384878 scopus 로고    scopus 로고
    • Alpha and 3(10): The split personality of polypeptide helices
    • Bolin K.A., Millhauser G.L. Alpha and 3(10): the split personality of polypeptide helices. Acc Chem Res. 32:1999;1027-1033.
    • (1999) Acc Chem Res , vol.32 , pp. 1027-1033
    • Bolin, K.A.1    Millhauser, G.L.2
  • 63
    • 0000466156 scopus 로고
    • Ab initio simulation of the vibrational circular dichroism of coupled peptides
    • Bour P., Keiderling T.A. Ab initio simulation of the vibrational circular dichroism of coupled peptides. J Am Chem Soc. 115:1993;9602-9607.
    • (1993) J Am Chem Soc , vol.115 , pp. 9602-9607
    • Bour, P.1    Keiderling, T.A.2
  • 64
    • 0034655810 scopus 로고    scopus 로고
    • Simulations of oligopeptide vibrational circular dichroism. Effects of isotopic labeling
    • Bour P., Kubelka J., Keiderling T.A. Simulations of oligopeptide vibrational circular dichroism. Effects of isotopic labeling. Biopolymers. 53:2000;380-395.
    • (2000) Biopolymers , vol.53 , pp. 380-395
    • Bour, P.1    Kubelka, J.2    Keiderling, T.A.3
  • 65
    • 0030556776 scopus 로고    scopus 로고
    • N-acetyl-l-alanine-N′-methylamide: A density functional analysis of the vibrational absorption and vibrational circular dichroism spectra
    • Jalkanen K.J., Suhai S. N-acetyl-l-alanine-N′-methylamide: a density functional analysis of the vibrational absorption and vibrational circular dichroism spectra. Chem Phys. 208:1996;81-116.
    • (1996) Chem Phys , vol.208 , pp. 81-116
    • Jalkanen, K.J.1    Suhai, S.2
  • 66
    • 0033482851 scopus 로고    scopus 로고
    • L-Alanyl-l-alanine in the zwitterionic state: Structures determined in the presence of explicit water molecules and with continuum models using density functional theory
    • Knapp-Mohammady M., Jalkanen K.J., Nardi F., Wade R.C., Suhai S. l-Alanyl-l-alanine in the zwitterionic state: structures determined in the presence of explicit water molecules and with continuum models using density functional theory. Chem Phys. 240:1999;63-77. For a small fully optimized peptide, explicit water effects on the IR and VCD spectra are calculated ab initio and compared with simulations using continuum models for solvent.
    • (1999) Chem Phys , vol.240 , pp. 63-77
    • Knapp-Mohammady, M.1    Jalkanen, K.J.2    Nardi, F.3    Wade, R.C.4    Suhai, S.5
  • 67
    • 0001167142 scopus 로고    scopus 로고
    • Transfer of molecular property tensors in Cartesian coordinates: A new algorithm for simulation of vibrational spectra
    • Bour P., Sopkova J., Bednarova L., Malon P., 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
    • Bour, P.1    Sopkova, J.2    Bednarova, L.3    Malon, P.4    Keiderling, T.A.5
  • 68
    • 0034819486 scopus 로고    scopus 로고
    • 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structures. An ab initio study
    • 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structures. An ab initio study. J Am Chem Soc. 123:2001;6142-6150.
    • (2001) J Am Chem Soc , vol.123 , pp. 6142-6150
    • Kubelka, J.1    Keiderling, T.A.2
  • 69
    • 0035418713 scopus 로고    scopus 로고
    • Neural-network analysis of the vibrational spectra of N-acetyl l-alanyl N′-methyl amide conformational states
    • Bohr H.G., Frimand K., Jalkanen K.J., Nieminen R.M., Suhai S. Neural-network analysis of the vibrational spectra of N-acetyl l-alanyl N′-methyl amide conformational states. Phys Rev E. 64:2001;1905.
    • (2001) Phys Rev E , vol.64 , pp. 1905
    • Bohr, H.G.1    Frimand, K.2    Jalkanen, K.J.3    Nieminen, R.M.4    Suhai, S.5
  • 70
    • 0034225123 scopus 로고    scopus 로고
    • Hybrid SCC-DFTB/molecular mechanical studies of H-bonded systems and of N-acetyl-(L-Ala) (n) N′-methylamide helices in water solution source
    • Han W.G., Elstner M., Jalkanen K.J., Frauenheim T., Suhai S. Hybrid SCC-DFTB/molecular mechanical studies of H-bonded systems and of N-acetyl-(L-Ala) (n) N′-methylamide helices in water solution source. Int J Quantum Chem. 78:2000;459-479.
    • (2000) Int J Quantum Chem , vol.78 , pp. 459-479
    • Han, W.G.1    Elstner, M.2    Jalkanen, K.J.3    Frauenheim, T.4    Suhai, S.5
  • 71
    • 0035819028 scopus 로고    scopus 로고
    • Ab initio calculation of amide carbonyl stretch vibrational frequencies in solution with modified basis sets. 1. N-methyl acetamide
    • Kubelka J., Keiderling T.A. Ab initio calculation of amide carbonyl stretch vibrational frequencies in solution with modified basis sets. 1. N-methyl acetamide. J Phys Chem. 105:2001;10922-10928.
    • (2001) J Phys Chem , vol.105 , pp. 10922-10928
    • Kubelka, J.1    Keiderling, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.