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Volumn 20, Issue 10, 2008, Pages 1104-1119

Vibrational circular dichroism and IR spectral analysis as a test of theoretical conformational modeling for a cyclic hexapeptide

Author keywords

Density functional theory; Infrared absorption; Molecular dynamics; Peptide conformational spectral interpretation; Solvent effects; Vibrational circular dichroism

Indexed keywords

CYCLOPEPTIDE; OLIGOPEPTIDE; SOLVENT;

EID: 58149173405     PISSN: 08990042     EISSN: 1520636X     Source Type: Journal    
DOI: 10.1002/chir.20560     Document Type: Article
Times cited : (24)

References (85)
  • 1
    • 0035356378 scopus 로고    scopus 로고
    • Determination of the absolute configuration of 1-(2-methylnaphtyl) methyl sulfoxide by vibrational circular dichroism spectroscopy
    • Aamouche A, Devlin FJ, Stephens PJ. Determination of the absolute configuration of 1-(2-methylnaphtyl) methyl sulfoxide by vibrational circular dichroism spectroscopy. J Org Chem 2001;66:3671-3677.
    • (2001) J Org Chem , vol.66 , pp. 3671-3677
    • Aamouche, A.1    Devlin, F.J.2    Stephens, P.J.3
  • 2
    • 26944447464 scopus 로고    scopus 로고
    • Spectral broadening and diffusion by torsional motion in biphenyl
    • Beenken WJD, Lischka H. Spectral broadening and diffusion by torsional motion in biphenyl. J Chem Phys 2005;123:144311.
    • (2005) J Chem Phys , vol.123 , pp. 144311
    • Beenken, W.J.D.1    Lischka, H.2
  • 3
    • 0019882126 scopus 로고
    • Determination of the secondary structure of proteins from the amide I band of the laser raman spectrum
    • Williams RW, Dunker AK. Determination of the secondary structure of proteins from the amide I band of the laser raman spectrum. J Mol Biol 1981;152:783-813.
    • (1981) J Mol Biol , vol.152 , pp. 783-813
    • Williams, R.W.1    Dunker, A.K.2
  • 4
    • 0036802313 scopus 로고    scopus 로고
    • Protein and peptide secondary structure and conformational determination with vibrational circular dichroism
    • Keiderling TA. Protein and peptide secondary structure and conformational determination with vibrational circular dichroism. Curr Opin Chem Biol 2002;6:682-688.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 682-688
    • Keiderling, T.A.1
  • 5
    • 0000042757 scopus 로고    scopus 로고
    • Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies
    • Berova N, Nakanishi K, Woody RW, editors, 2nd ed. New York: Wiley-VCH
    • Keiderling TA. Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies. In: Berova N, Nakanishi K, Woody RW, editors. Circular dichroism: principles and applications, 2nd ed. New York: Wiley-VCH; 2000. p 621-666.
    • (2000) Circular Dichroism: Principles and Applications , pp. 621-666
    • Keiderling, T.A.1
  • 6
    • 33749573474 scopus 로고    scopus 로고
    • Raman optical activity: An incisive probe of chirality and of biomolecular structure and behaviour
    • Barron LD, Zhu F, Hecht L. Raman optical activity: an incisive probe of chirality and of biomolecular structure and behaviour. Vib Spectrosc 2006;42:15-24.
    • (2006) Vib Spectrosc , vol.42 , pp. 15-24
    • Barron, L.D.1    Zhu, F.2    Hecht, L.3
  • 7
    • 0033596301 scopus 로고    scopus 로고
    • Isotope-edited FTIR spectroscopy of helical peptides
    • Decatur SM, Antonic J. Isotope-edited FTIR spectroscopy of helical peptides. J Am Chem Soc 1999;121:11914-11915.
    • (1999) J Am Chem Soc , vol.121 , pp. 11914-11915
    • Decatur, S.M.1    Antonic, J.2
  • 10
    • 0242490659 scopus 로고    scopus 로고
    • The organization and assembly of a beta-sheet formed by a prion peptide in solution: An isotope-edited FTIR study
    • Silva RAGD, Barber-Armstrong W, Decatur SM. The organization and assembly of a beta-sheet formed by a prion peptide in solution: an isotope-edited FTIR study. J Am Chem Soc 2003;125:13674-13675.
    • (2003) J Am Chem Soc , vol.125 , pp. 13674-13675
    • Silva, R.A.G.D.1    Barber-Armstrong, W.2    Decatur, S.M.3
  • 11
    • 0037168451 scopus 로고    scopus 로고
    • Probing the effect of side chains on the conformaiton and stability of helical peptides via isotope-edited infrared spectroscopy
    • Silva RAGD, Nguyen JY, Decatur SM. Probing the effect of side chains on the conformaiton and stability of helical peptides via isotope-edited infrared spectroscopy. Biochemistry 2002;51:15296-15303.
    • (2002) Biochemistry , vol.51 , pp. 15296-15303
    • Silva, R.A.G.D.1    Nguyen, J.Y.2    Decatur, S.M.3
  • 12
    • 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. In: Hicks JM, editor. Chirality: Physical chemistry
    • Washington DC: American Chemical Society
    • Kubelka J, Silva RAGD, Bouř P, Decatur SM, Keiderling TA. Chirality in peptide vibrations. Ab Initio computational studies of length, solvation, hydrogen bond, dipole coupling and isotope effects on vibrational CD. In: Hicks JM, editor. Chirality: physical chemistry. ACS Symposium Series. Vol. 810. Washington DC: American Chemical Society; 2002. p 50-64.
    • (2002) ACS Symposium Series , vol.810 , pp. 50-64
    • Kubelka, J.1    Silva, R.A.G.D.2    Bouř, P.3    Decatur, S.M.4    Keiderling, T.A.5
  • 13
    • 0034819486 scopus 로고    scopus 로고
    • 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structurres
    • 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structurres. An ab initio study. J Am Chem Soc 2001;123:6142-6150.
    • (2001) An Ab Initio Study. J Am Chem Soc , vol.123 , pp. 6142-6150
    • Kubelka, J.1    Keiderling, T.A.2
  • 14
    • 0034682537 scopus 로고    scopus 로고
    • Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution
    • Silva RAGD, Kubelka J, Decatur SM, Bouř P, Keiderling TA. Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution. Proc Natl Acad Sci USA 2000;97:8318-8323.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8318-8323
    • Silva, R.A.G.D.1    Kubelka, J.2    Decatur, S.M.3    Bouř, P.4    Keiderling, T.A.5
  • 15
    • 0034285165 scopus 로고    scopus 로고
    • IR spectroscopy of isotope-labeled helical peptides: Probing the effect of N-acetylation on helix stability
    • Decatur SM. IR spectroscopy of isotope-labeled helical peptides: probing the effect of N-acetylation on helix stability. Biopolymers 2000;54:180-185.
    • (2000) Biopolymers , vol.54 , pp. 180-185
    • Decatur, S.M.1
  • 16
    • 11844262057 scopus 로고    scopus 로고
    • Spectroscopic evidence for backbone desolvation of helical peptides by 2, 2, 2-trifluoroethanol: An isotope edited IR study
    • Starzyk A, Barber-Armstrong W, Sridharan M, Decatur SM. Spectroscopic evidence for backbone desolvation of helical peptides by 2, 2, 2-trifluoroethanol: an isotope edited IR study. Biochemistry 2005;44:369-376.
    • (2005) Biochemistry , vol.44 , pp. 369-376
    • Starzyk, A.1    Barber-Armstrong, W.2    Sridharan, M.3    Decatur, S.M.4
  • 17
    • 15744398699 scopus 로고    scopus 로고
    • Ab initio modeling of amide I coupling in antiparallel beta-sheets and the effect of 13C isotopic labeling on infrared spectra
    • Bouř P, Keiderling TA. Ab initio modeling of amide I coupling in antiparallel beta-sheets and the effect of 13C isotopic labeling on infrared spectra. J Phys Chem B 2005;109:5348-5357.
    • (2005) J Phys Chem B , vol.109 , pp. 5348-5357
    • Bouř, P.1    Keiderling, T.A.2
  • 18
    • 33645517136 scopus 로고    scopus 로고
    • Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy
    • Decatur SM. Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy. Acc Chem Res 2006;39:169-175.
    • (2006) Acc Chem Res , vol.39 , pp. 169-175
    • Decatur, S.M.1
  • 19
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy-combining variable selection principle and cluster analyses with neural network, ridge regression and self-consistent methods
    • Sreerama N, Woody RW. Protein secondary structure from circular dichroism spectroscopy-combining variable selection principle and cluster analyses with neural network, ridge regression and self-consistent methods. J Mol Biol 1994;242:497-507.
    • (1994) J Mol Biol , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 21
    • 18444365588 scopus 로고    scopus 로고
    • Solvent effects on IR and VCD spectra of helical peptides: DFT-based static spectral simulations with explicit water
    • Kubelka J, Huang R, Keiderling TA. Solvent effects on IR and VCD spectra of helical peptides: DFT-based static spectral simulations with explicit water. J Phys Chem B 2005;109:8231-8243.
    • (2005) J Phys Chem B , vol.109 , pp. 8231-8243
    • Kubelka, J.1    Huang, R.2    Keiderling, T.A.3
  • 23
    • 0345735101 scopus 로고    scopus 로고
    • FTIR and CD spectroscopic studies on cyclic penta- and hexa-peptides. Detailed examination of hydrogen bonding in (beta) - and (gamma) - Turns determined by NMR
    • Vass E, Kurz M, Konat RK, Hollosi M. FTIR and CD spectroscopic studies on cyclic penta- and hexa-peptides. Detailed examination of hydrogen bonding in (beta) - and (gamma) - turns determined by NMR. Spectrochim Acta 1998;54:773-786.
    • (1998) Spectrochim Acta , vol.54 , pp. 773-786
    • Vass, E.1    Kurz, M.2    Konat, R.K.3    Hollosi, M.4
  • 25
    • 0038281274 scopus 로고    scopus 로고
    • Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins
    • Vass E, Hollosi M, Besson F, Buchet R. Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins. Chem Rev 2003;103:1917-1954.
    • (2003) Chem Rev , vol.103 , pp. 1917-1954
    • Vass, E.1    Hollosi, M.2    Besson, F.3    Buchet, R.4
  • 26
    • 37549028734 scopus 로고    scopus 로고
    • Tight β-turns in peptides. DFT-based study of infrared absorption and vibrational circular dichroism for various conformers including solvent effects
    • Kim J, Kapitán J, Lakhani A, Bouř P, Keiderling TA. Tight β-turns in peptides. DFT-based study of infrared absorption and vibrational circular dichroism for various conformers including solvent effects. Theor Chem Acc 2008;119:81-97.
    • (2008) Theor Chem Acc , vol.119 , pp. 81-97
    • Kim, J.1    Kapitán, J.2    Lakhani, A.3    Bouř, P.4    Keiderling, T.A.5
  • 27
    • 33847158264 scopus 로고    scopus 로고
    • Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine
    • Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des 2007;69:31-40.
    • (2007) Chem Biol Drug des , vol.69 , pp. 31-40
    • Krishnan, B.1    Szymanska, A.2    Gierasch, L.M.3
  • 28
    • 33646023145 scopus 로고    scopus 로고
    • Hybrid peptide hairpins containing alpha- and omega-amino acids: Conformational analysis of decapeptides with unsubstituted beta-, gamma-, and deltaresidues at positions 3 and 8
    • Roy RS, Gopi HN, Raghothama S, Karle IL, Balaram P. Hybrid peptide hairpins containing alpha- and omega-amino acids: conformational analysis of decapeptides with unsubstituted beta-, gamma-, and deltaresidues at positions 3 and 8. Chem A Eur J 2006;12:3295-3302.
    • (2006) Chem a Eur J , vol.12 , pp. 3295-3302
    • Roy, R.S.1    Gopi, H.N.2    Raghothama, S.3    Karle, I.L.4    Balaram, P.5
  • 29
    • 31944446531 scopus 로고    scopus 로고
    • NMR analysis of aromatic interactions in designed peptide beta-hairpins
    • Mahalakshmi R, Raghothama S, Balaram P. NMR analysis of aromatic interactions in designed peptide beta-hairpins. J Am Chem Soc 2006;128:1125-1138.
    • (2006) J Am Chem Soc , vol.128 , pp. 1125-1138
    • Mahalakshmi, R.1    Raghothama, S.2    Balaram, P.3
  • 30
    • 0037436347 scopus 로고    scopus 로고
    • Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets
    • Syud FA, Stanger HE, Mortell HS, Espinosa JF, Fisk JD, Fry CG, Gellman SH. Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets. J Mol Biol 2003;326:553-568.
    • (2003) J Mol Biol , vol.326 , pp. 553-568
    • Syud, F.A.1    Stanger, H.E.2    Mortell, H.S.3    Espinosa, J.F.4    Fisk, J.D.5    Fry, C.G.6    Gellman, S.H.7
  • 31
    • 0037117523 scopus 로고    scopus 로고
    • Infinite pleated beta-sheet formed by the beta-hairpin Boc-beta-Phe-beta-Phe-D-Pro-Gly-beta-Phe-beta-Phe-OMe
    • Karle I, Gopi HN, Balaram P. Infinite pleated beta-sheet formed by the beta-hairpin Boc-beta-Phe-beta-Phe-D-Pro-Gly-beta-Phe-beta-Phe-OMe. Proc Natl Acad Sci USA 2002;99:5160-5164.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5160-5164
    • Karle, I.1    Gopi, H.N.2    Balaram, P.3
  • 35
    • 2642670311 scopus 로고    scopus 로고
    • Design of a 20-amino acid, three-stranded beta-sheet protein
    • Kortemme T, Ramirez-Alvarado M, Serrano L. Design of a 20-amino acid, three-stranded beta-sheet protein. Science 1998;281:253-256.
    • (1998) Science , vol.281 , pp. 253-256
    • Kortemme, T.1    Ramirez-Alvarado, M.2    Serrano, L.3
  • 37
    • 0036113724 scopus 로고    scopus 로고
    • Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet
    • Espinosa JF, Syud FA, Gellman SH. Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet. Protein Sci 2002;11:1492-1505.
    • (2002) Protein Sci , vol.11 , pp. 1492-1505
    • Espinosa, J.F.1    Syud, F.A.2    Gellman, S.H.3
  • 38
    • 0038546798 scopus 로고    scopus 로고
    • Optical spectroscopic investigations of model beta-sheet hairpins in aqueous solution
    • Hilario J, Kubelka J, Keiderling TA. Optical spectroscopic investigations of model beta-sheet hairpins in aqueous solution. J Am Chem Soc 2003;125:7562-7574.
    • (2003) J Am Chem Soc , vol.125 , pp. 7562-7574
    • Hilario, J.1    Kubelka, J.2    Keiderling, T.A.3
  • 39
    • 0032939806 scopus 로고    scopus 로고
    • WW: An isolated threestranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state
    • Koepf EK, Petrassi HM, Sudol M, Kelly JW. WW: an isolated threestranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state. Protein Sci 1999;8:841-853.
    • (1999) Protein Sci , vol.8 , pp. 841-853
    • Koepf, E.K.1    Petrassi, H.M.2    Sudol, M.3    Kelly, J.W.4
  • 40
    • 30544437694 scopus 로고    scopus 로고
    • Vibrational spectral simulation for peptides of mixed secondary structure: Method comparisons with the Trpzip model hairpin
    • Bouř P, Keiderling TA. Vibrational spectral simulation for peptides of mixed secondary structure: method comparisons with the Trpzip model hairpin. J Phys Chem B 2005;109:23687-23697.
    • (2005) J Phys Chem B , vol.109 , pp. 23687-23697
    • Bouř, P.1    Keiderling, T.A.2
  • 41
    • 28944446881 scopus 로고    scopus 로고
    • A complete set of NMR chemical shifts and spin-spin coupling constants for L-alanyl-L-alanine zwitterion and analysis of its conformational behavior
    • Bouř P, Buděšínský M, Špirko V, Kapitán J, Šebestík J, Sychrovský V. A complete set of NMR chemical shifts and spin-spin coupling constants for L-alanyl-L-alanine zwitterion and analysis of its conformational behavior. J Am Chem Soc 2005;127:17079-17089.
    • (2005) J Am Chem Soc , vol.127 , pp. 17079-17089
    • Bouř, P.1    Buděšínský, M.2    Špirko, V.3    Kapitán, J.4    Šebestík, J.5    Sychrovský, V.6
  • 43
    • 0027551639 scopus 로고
    • Characterization of β-turns in cyclic hexapeptides in solution by Fourier transform IR spectroscopy
    • Mantsch HH, Perczel A, Hollosi M, Fasman GD. Characterization of β-turns in cyclic hexapeptides in solution by Fourier transform IR spectroscopy. Biopolymers 1993;33:201-207.
    • (1993) Biopolymers , vol.33 , pp. 201-207
    • Mantsch, H.H.1    Perczel, A.2    Hollosi, M.3    Fasman, G.D.4
  • 44
  • 46
    • 0021114870 scopus 로고
    • Cyclic peptide disulfides. Consecutive beta-turn conformation of a synthetic model peptide corresponding to the active site of thioredoxin
    • Ravi A, Balaram P. Cyclic peptide disulfides. Consecutive beta-turn conformation of a synthetic model peptide corresponding to the active site of thioredoxin. Biochi Biophys Acta 1983;745:301-309.
    • (1983) Biochi Biophys Acta , vol.745 , pp. 301-309
    • Ravi, A.1    Balaram, P.2
  • 48
    • 0037438384 scopus 로고    scopus 로고
    • Stability of cyclic beta-hairpins: Asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair
    • Russell SJ, Blandl T, Skelton NJ, Cochran AG. Stability of cyclic beta-hairpins: asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair. J Am Chem Soc 2003;125:388-395.
    • (2003) J Am Chem Soc , vol.125 , pp. 388-395
    • Russell, S.J.1    Blandl, T.2    Skelton, N.J.3    Cochran, A.G.4
  • 49
    • 0000644502 scopus 로고
    • Cyclic peptide disulfides-solution and solid-state conformation of Boc-Cys-Pro-Aib-Cys-S-S-bridge-NH-Me, a disulfide-bridged peptide helix
    • Ravi A, Prasad BVV, Balaram P. Cyclic peptide disulfides-solution and solid-state conformation of Boc-Cys-Pro-Aib-Cys-S-S-bridge-NH-Me, a disulfide-bridged peptide helix. J Am Chem Soc 1983;105:105-109.
    • (1983) J Am Chem Soc , vol.105 , pp. 105-109
    • Ravi, A.1    Prasad, B.V.V.2    Balaram, P.3
  • 50
    • 0028982307 scopus 로고
    • Conformational studies of β-turns in cyclic peptides by vibrational CD
    • Xie P, Zhou QW, Diem M. Conformational studies of β-turns in cyclic peptides by vibrational CD. J Am Chem Soc 1995;117:9502-9508.
    • (1995) J Am Chem Soc , vol.117 , pp. 9502-9508
    • Xie, P.1    Zhou, Q.W.2    Diem, M.3
  • 52
    • 2042487484 scopus 로고
    • Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of Type I and Type II beta-turns
    • Perczel A, Hollosi M, Foxman BM, Fasman GD. Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of Type I and Type II beta-turns. J Am Chem Soc 1991;113:9772-9784.
    • (1991) J Am Chem Soc , vol.113 , pp. 9772-9784
    • Perczel, A.1    Hollosi, M.2    Foxman, B.M.3    Fasman, G.D.4
  • 53
    • 0028920302 scopus 로고
    • Structures, dynamics, and biological activities of 15 cyclic hexapeptide analogs of the alpha-amylase inhibitor tendamistat (HOE 467) in solution
    • Matter H, Kessler H. Structures, dynamics, and biological activities of 15 cyclic hexapeptide analogs of the alpha-amylase inhibitor tendamistat (HOE 467) in solution. J Am Chem Soc 1995;117:3347-3359.
    • (1995) J Am Chem Soc , vol.117 , pp. 3347-3359
    • Matter, H.1    Kessler, H.2
  • 54
    • 0033541110 scopus 로고    scopus 로고
    • Beta-turn and beta-hairpin mimicry with tetrasubstituted alkenes
    • Gardner RR, Liang GB, Gellman SH. Beta-turn and beta-hairpin mimicry with tetrasubstituted alkenes. J Am Chem Soc 1999;121:1806-1816.
    • (1999) J Am Chem Soc , vol.121 , pp. 1806-1816
    • Gardner, R.R.1    Liang, G.B.2    Gellman, S.H.3
  • 55
    • 0034805437 scopus 로고    scopus 로고
    • Incorporating beta-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded beta-sheets
    • Kaul R, Angeles AR, Jager M, Powers ET, Kelly JW. Incorporating beta-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded beta-sheets. J Am Chem Soc 2001;123:5206-5212.
    • (2001) J Am Chem Soc , vol.123 , pp. 5206-5212
    • Kaul, R.1    Angeles, A.R.2    Jager, M.3    Powers, E.T.4    Kelly, J.W.5
  • 56
    • 0035850529 scopus 로고    scopus 로고
    • Interstrand side chain-side chain interactions in a designed β-hairpin: Significance of both lateral and diagonal pairings
    • Syud FA, Stanger HE, Gellman SH. Interstrand side chain-side chain interactions in a designed β-hairpin: significance of both lateral and diagonal pairings. J Am Chem Soc 2001;123:8667-8677.
    • (2001) J Am Chem Soc , vol.123 , pp. 8667-8677
    • Syud, F.A.1    Stanger, H.E.2    Gellman, S.H.3
  • 58
    • 33845309676 scopus 로고    scopus 로고
    • N-methylated cyclic pentaalanine peptides as template structures
    • Chatterjee J, Mierke D, Kessler H. N-methylated cyclic pentaalanine peptides as template structures. J Am Chem Soc 2006;128:15164-15172.
    • (2006) J Am Chem Soc , vol.128 , pp. 15164-15172
    • Chatterjee, J.1    Mierke, D.2    Kessler, H.3
  • 59
    • 0023841714 scopus 로고
    • Peptide conformations. 46. Conformational analysis of a superpotent cytoprotective cyclic somatostatin analog
    • Kessler H, Bats JW, Griesinger C, Koll S, Will M, Wagner K. Peptide conformations. 46. Conformational analysis of a superpotent cytoprotective cyclic somatostatin analog. J Am Chem Soc 1988;110:1033-1049.
    • (1988) J Am Chem Soc , vol.110 , pp. 1033-1049
    • Kessler, H.1    Bats, J.W.2    Griesinger, C.3    Koll, S.4    Will, M.5    Wagner, K.6
  • 60
    • 0019872602 scopus 로고
    • Conformations of (X-L-Pro-Y) 2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins
    • Gierasch LM, Deber CM, Madison V, Niu CH, Blout ER. Conformations of (X-L-Pro-Y) 2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. Biochemistry 1981;20:4730-4738.
    • (1981) Biochemistry , vol.20 , pp. 4730-4738
    • Gierasch, L.M.1    Deber, C.M.2    Madison, V.3    Niu, C.H.4    Blout, E.R.5
  • 61
    • 0000032313 scopus 로고
    • Conformational analysis of cyclic hexapeptides containing the D-Pro-L-Pro sequence to fix beta-turn positions
    • Bean JW, Kopple KD, Peishoff CE. Conformational analysis of cyclic hexapeptides containing the D-Pro-L-Pro sequence to fix beta-turn positions. J Am Chem Soc 1992;114:5328-5334.
    • (1992) J Am Chem Soc , vol.114 , pp. 5328-5334
    • Bean, J.W.1    Kopple, K.D.2    Peishoff, C.E.3
  • 62
    • 0027537248 scopus 로고
    • BetaVI turns in peptides and proteins: A model peptide mimicry
    • Muller G, Gurrath M, Kurz M, Kessler H. BetaVI turns in peptides and proteins: a model peptide mimicry. Protein Struct 1993;15:235-251.
    • (1993) Protein Struct , vol.15 , pp. 235-251
    • Muller, G.1    Gurrath, M.2    Kurz, M.3    Kessler, H.4
  • 63
    • 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 TA. 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 2001;123:12048-12058.
    • (2001) J Am Chem Soc , vol.123 , pp. 12048-12058
    • Kubelka, J.1    Keiderling, T.A.2
  • 64
    • 35948936905 scopus 로고    scopus 로고
    • Cross-strand coupling of a β-hairpin peptide stabilized with an Aib-Gly turn using isotope-edited IR spectroscopy
    • Huang R, Setnička V, Etienne MA, Kim J, Kubelka J, Hammer RP, Keiderling TA. Cross-strand coupling of a β-hairpin peptide stabilized with an Aib-Gly turn using isotope-edited IR spectroscopy. J Am Chem Soc 2007;129:13592-13603.
    • (2007) J Am Chem Soc , vol.129 , pp. 13592-13603
    • Huang, R.1    Setnička, V.2    Etienne, M.A.3    Kim, J.4    Kubelka, J.5    Hammer, R.P.6    Keiderling, T.A.7
  • 65
    • 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, Keiderling TA. Transfer of molecular property tensors in Cartesian coordinates: a new algorithm for simulation of vibrational spectra. J Comput Chem 1997;18:646-659.
    • (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
  • 66
    • 33846117544 scopus 로고    scopus 로고
    • Simulation of infrared spectra for beta-hairpin peptides stabilized by an Aib-Gly turn sequence: Correlation between conformational fluctuation and vibrational coupling
    • Kim J, Huang R, Kubelka J, Bouř P, Keiderling TA. Simulation of infrared spectra for beta-hairpin peptides stabilized by an Aib-Gly turn sequence: correlation between conformational fluctuation and vibrational coupling. J Phys Chem B 2006;110:23590-23602.
    • (2006) J Phys Chem B , vol.110 , pp. 23590-23602
    • Kim, J.1    Huang, R.2    Kubelka, J.3    Bouř, P.4    Keiderling, T.A.5
  • 67
    • 33644531529 scopus 로고    scopus 로고
    • Demonstration of the ring conformation in polyproline by the Raman optical activity
    • Kapitán J, Baumruk V, Kopecký VJ, Bouř P. Demonstration of the ring conformation in polyproline by the Raman optical activity. J Am Chem Soc 2006;128:2438-2443.
    • (2006) J Am Chem Soc , vol.128 , pp. 2438-2443
    • Kapitán, J.1    Baumruk, V.2    Kopecký, V.J.3    Bouř, P.4
  • 68
    • 0000331105 scopus 로고    scopus 로고
    • Computations of the Raman optical activity via the sum-overstates expansions
    • Bouř P. Computations of the Raman optical activity via the sum-overstates expansions. J Comput Chem 2001;22:426-435.
    • (2001) J Comput Chem , vol.22 , pp. 426-435
    • Bouř, P.1
  • 69
    • 0000886123 scopus 로고
    • A 3-dimensional orthogonal protection scheme for solid-phase peptide-synthesis under mild conditions
    • Barany G, Albericio F. A 3-dimensional orthogonal protection scheme for solid-phase peptide-synthesis under mild conditions. J Am Chem Soc 1985;107:4936-4942.
    • (1985) J Am Chem Soc , vol.107 , pp. 4936-4942
    • Barany, G.1    Albericio, F.2
  • 70
    • 0027406752 scopus 로고
    • A novel, convenient, 3-dimensional orthogonal strategy for solidphase synthesis of cyclic-peptides
    • Kates SA, Sole NA, Johnson CR, Hudson D, Barany G, Albericio F. A novel, convenient, 3-dimensional orthogonal strategy for solidphase synthesis of cyclic-peptides. Tetrahedron Lett 1993;34:1549-1552.
    • (1993) Tetrahedron Lett , vol.34 , pp. 1549-1552
    • Kates, S.A.1    Sole, N.A.2    Johnson, C.R.3    Hudson, D.4    Barany, G.5    Albericio, F.6
  • 72
    • 85130650550 scopus 로고    scopus 로고
    • Vibrational circular dichroism of biopolymers. Summary of methods and applications
    • Braiman M, Gregoriou V, editors, Boca Raton: CRC Press
    • Keiderling TA, Kubelka J, Hilario J. Vibrational circular dichroism of biopolymers. Summary of methods and applications. In: Braiman M, Gregoriou V, editors. Vibrational spectroscopy of polymers and biological systems. Boca Raton: CRC Press; 2006. p 253-324.
    • (2006) Vibrational Spectroscopy of Polymers and Biological Systems , pp. 253-324
    • Keiderling, T.A.1    Kubelka, J.2    Hilario, J.3
  • 74
    • 0029633186 scopus 로고
    • AMBER, a package of computer progeams for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE, Debolt S, Ferguson DM, Seibel G, Kollman PA. AMBER, a package of computer progeams for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp Phys Commun 1995;91:1-41.
    • (1995) Comp Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    Debolt, S.6    Ferguson, D.M.7    Seibel, G.8    Kollman, P.A.9
  • 75
    • 0004016501 scopus 로고
    • Comparison of simple potential fuctions for simulating liquid water
    • Jorgensen WL, Chandrasekhar J, Madura JD. Comparison of simple potential fuctions for simulating liquid water. J Chem Phys 1983;79:926-935.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 77
    • 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, Keiderling TA. Partial optimization of molecular geometry in normal coordinates and use as a tool for simulation of vibrational spectra. J Chem Phys 2002;117:4126-4132.
    • (2002) J Chem Phys , vol.117 , pp. 4126-4132
    • Bouř, P.1    Keiderling, T.A.2
  • 78
    • 28844440942 scopus 로고    scopus 로고
    • Convergence properties of the normal mode optimization and its combination with molecular geometry constraints
    • Bouř P. Convergence properties of the normal mode optimization and its combination with molecular geometry constraints. Collect Czech Chem Commun 2005;70:1315-1340.
    • (2005) Collect Czech Chem Commun , vol.70 , pp. 1315-1340
    • Bouř, P.1
  • 79
    • 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 TA. Ab initio calculation of amide carbonyl stretch vibrational frequencies in solution with modified basis sets. 1. N-methyl acetamide. J Phys Chem A 2001;105:10922-10928.
    • (2001) J Phys Chem A , vol.105 , pp. 10922-10928
    • Kubelka, J.1    Keiderling, T.A.2
  • 80
    • 20844436194 scopus 로고    scopus 로고
    • Empirical solvent correction for multiple amide group vibrational modes
    • Bouř P, Michalík D, Kapitán J. Empirical solvent correction for multiple amide group vibrational modes. J Chem Phys 2005;122:144501.
    • (2005) J Chem Phys , vol.122 , pp. 144501
    • Bouř, P.1    Michalík, D.2    Kapitán, J.3
  • 81
    • 8344267908 scopus 로고    scopus 로고
    • On the influence of the water electrostatic field on the amide group vibrational frequencies
    • Bouř P. On the influence of the water electrostatic field on the amide group vibrational frequencies. J Chem Phys 2004;121:7545-7548.
    • (2004) J Chem Phys , vol.121 , pp. 7545-7548
    • Bouř, P.1
  • 82
    • 0037093868 scopus 로고    scopus 로고
    • 10- and α-helices. Theoretical analysis of the impact of α-methyl substitution on experimental spectra
    • 10- and α-helices. Theoretical analysis of the impact of α-methyl substitution on experimental spectra. J Am Chem Soc 2002;124:5325-5332.
    • (2002) J Am Chem Soc , vol.124 , pp. 5325-5332
    • Kubelka, J.1    Silva, R.A.G.D.2    Keiderling, T.A.3
  • 83
    • 0037026869 scopus 로고    scopus 로고
    • Quantum mechanical models of peptide helices and their vibrational spectra
    • Bouř P, Kubelka J, Keiderling TA. Quantum mechanical models of peptide helices and their vibrational spectra. Biopolymers 2002;65:45-69.
    • (2002) Biopolymers , vol.65 , pp. 45-69
    • Bouř, P.1    Kubelka, J.2    Keiderling, T.A.3
  • 84
    • 84961981133 scopus 로고    scopus 로고
    • Empirical modeling of the peptide amide I band IR intensity in water solution
    • Bouř P, Keiderling TA. Empirical modeling of the peptide amide I band IR intensity in water solution. J Chem Phys 2003;119:11253-11262.
    • (2003) J Chem Phys , vol.119 , pp. 11253-11262
    • Bouř, P.1    Keiderling, T.A.2
  • 85
    • 33646228036 scopus 로고    scopus 로고
    • IR spectra of N-methylacetamide in water predicted by combined quantum mechanical/molecular mechanical molecular dynamics simulations
    • Yang S, Cho M. IR spectra of N-methylacetamide in water predicted by combined quantum mechanical/molecular mechanical molecular dynamics simulations. J Chem Phys 2005;123:134503.
    • (2005) J Chem Phys , vol.123 , pp. 134503
    • Yang, S.1    Cho, M.2


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