Carbonyl vibration resonance interactions in collagen structures
Keywords:
collagen, triple helix, resonance interactions, dipole-dipole approximation, perturbation theory, energy of stabilization, IR spectroscopy
Abstract
Resonance interaction of the carbonyl vibrations for model collagen structure [(PRO-PRO-GLY)10]3 have been treated on the basis of molecular exciton theory in a dipole-dipole approximation. The frequency shifts of the carbonyl vibrations induced by dipole coupling, inter-peptide and peptide-water hydrogen bond formation were obtained. The relative contributions of energies of peptide-water and inter-peptide hydrogen bonds and energies of other types of interaction to the total stabilization energy were estimated for the model collagen structures.
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References
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Basharov MA, Volkenshtein MV, Golovanov IB, Lazarev IuN, Sobolev VM. Nπ-sviazi v amidakh i peptidakh. Dokl. AN SSSR. 1986;287:211-5. (in Russian)
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Gasan AL, Maleev VYa, Semenov MA. Role of water in stabilizing the helical biomacromolecules DNA and collagen. Studia. Biophysica. 1990;136(2-3):171-8.
Engle J, Chen H-T, Prockop DJ. The triple helix-coil conversion of collagen-like polytripeptides in aqueous and nonagueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n. Biopolymers. 1977;16:601-22.
Eliot A. Infrakrasnye spektry i struktura polimerov. M.:Mir; 1972. (in Russian)
Lazarev YuA, Chishkovsky BA, Chromova TB. Amid I band of IR spectrum and structure of collagen and related polypeptides. Biopolymers. 1985;24(7):1449-78.
Yonath A, Traub W. Polymers of as collagen models IV. Structure analysis of poly (L-proly-glycy-L-prolyne). J. Molecular Biol. 1969;43(3):461-77.
Okuyuma K, Arnott S. Crystal and molecular structure of a collagen-like polypeptide (pro-pro-gly)10. J. Mol. Biol. 1981;152(2):427-43.
Lazarev IuA. Strukturoobrazovanie spirali kollagenovogo tipa v sinteticheskikh oligo- i politripeptidakh. Dis. dok. fiz.-mat. Nauk, Moskva, MGU, 1987.
Miyazawa TJ. Pertubation treatment of the characteristic vibrations of polypeptide chains in various configuraytions. J. Chem. Phys. 1960;32:1647-52.
Krimm S, Abe Y. Intermolecular interaction effects in the Amide I vibrations of B polypeptides. Proc. Nat. Acad. Sci. USA. 1972;69(10):2788-92.
Chirgadze IuN, Nevskaia NA. Rezonansnye vzaimodeistviia osnovnykh amidnykh kolebanii v uporiadochennykh peptidnykh strukturakh. Dokl. AN SSSR. 1973;208(2):447-50.
Fukushima K, Jdeguchi Y, Miyazawa T. The normal vibrations of polyglycine I. Bull. Chem. Soc. Japan. 1963;36:1301-7.
Semenov MA, Bolbuch TV. Carbonyl vibration resonance interactions helical polynucleotides Poly(dA)-Poly(dT) and PolyG-PolyC. Studia biophysica. 1984;102(3):215-20.
Semenov MA, Bereznyak EG. Hydration and stability of nucleic acids in the condenced state. Comments Mol. Cel. Biophys. 2000;10(1):1-23.
Davydov AS. Teoriia pogloshcheniia sveta v molekuliarnykh kristallakh. Kiev: AN USSR; 1951.
Semenov MA, Bolbukh TV. Rezonansnye vzaimodeistviia karbonilnykh kolebanii v spiralnykh polipeptidakh. Kharkov; 1982. p.28.
Berisio R, Vitagliano L, Mazzarella L, Zagari A. rystal structure of the collagen triple helix model [(PRO-PRO-GLY)10)3. Protein Sci.2002;11:262-70.
Gribov LA. Teoriia infrakrasnykh spektrov polimerov. M.:Nauka; 1977. (in Russian)
Basharov MA, Volkenshtein MV, Golovanov IB, Lazarev IuN, Sobolev VM. Nπ-sviazi v amidakh i peptidakh. Dokl. AN SSSR. 1986;287:211-5. (in Russian)
Semenov MA. Gidratatciia i strukturnoe sostoianie nukleinovykh kislot v kondensirovannom sostoianii. Dis. dok. fiz.-mat. nauk. Moskva:MGU. 1990. (in Russian)
Gasan AL, Maleev VYa, Semenov MA. Role of water in stabilizing the helical biomacromolecules DNA and collagen. Studia. Biophysica. 1990;136(2-3):171-8.
Engle J, Chen H-T, Prockop DJ. The triple helix-coil conversion of collagen-like polytripeptides in aqueous and nonagueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n. Biopolymers. 1977;16:601-22.
Published
2018-06-25
Cited
How to Cite
Melezhik, Y. P., & Semenov, M. A. (2018). Carbonyl vibration resonance interactions in collagen structures. Biophysical Bulletin, 2(13), 62-67. Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/12411
Section
Molecular biophysics
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