Stretching vibrations of carbonyl groups in raman spectra of collagen and poly(Gly-Pro-Pro): calcullation and experiment
Abstract
Raman spectra of poly(Gly-Pro-Pro) and type I collagen in deuterium oxide solution were obtained. Frequencies of type A stretching carbonyl vibrations were calculated according to the model of weakly connected oscillators within the limits of theory of perturbations for polypeptide structures taking into consideration the dynamic resonance interactions of transition dipoles. The calculated frequencies agree with the experimental frequencies of the Amide I band in Raman spectra of poly(Gly-Pro-Pro) and type I collagen.
Downloads
References
Eliot A. Infrakrasnye spektry i struktura polimerov. M.:Mir; 1972. (in Russian)
Miyazawa TJ. Pertubation treatment of the characteristic vibrations of polypeptide chains in various configurations. J. Chem. Phys. 1960;32:1647-52.
Chirgadze YuN, Nevskaya NA. Infrared Spectra and resonance interactions of Amide-I vibration of the antiparallel-chain pleated sheet. Biopolymers. 1976;15:607-25.
Chirgadze YaN, Nevskay NA. Infarared spectra and resonance interactions of Amide-I vibration of the parallel-chain pleated sheet. Biopolymers. 1976;15:627-36.
Nevskaya NA. Chirgadze YuN. Infrared spectra and resonance interactions of Amide-l and II vibrations a-helix. Biopolymers. 1976;15:637-48.
Moore WH, Krimm S. Vibrational analysis of peptides, polypeptides and proteins. I. Polyglycine I. Biopolymers. 1976;15:2439-64.
Moore WH, Krimm S. Vibrational analysis of peptides, polypeptides and proteins. II. β-Poly(L-alanine) and β-Poly (L-alanilglycine). Biopolymers. 1976;15:2465-83.
Melezhik EP,Semenov MA. Rezonansnye vzaimodeistviia karbonilnykh kolebanii v kollagenovykh strukturakh. Biofizicheskii vestnik. 2003;606(13):62-8. (in Russian)
Melezhik EP, Semenov MA, Ivanov AIu. Issledovanie tonkoi struktury polos Amid I IK-Fure spektra kollagena. Biofizicheskii vestnik. 2005;665(15):35-42. (in Russian)
Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple-helical structure. Nature Structural Biology. 1999;6(5):454-7.
Emsley J, Knight CG, Farndale RW, Barmes MJ, Liddington RC. Structural basis of collagen recognition by integrin a2b1. Cell. 2000;100:47-56.
Parker FS. Application of Infrared, Raman and resonance Raman spectroscopy in biochemistry. New York: Plemun Press; 1983. 550p.
Lazarev YA, Grishkovsky BA, Khromova TB, Lazareva AV, Grechishko VS. Bound water in the collagen-like triple-helical structure. Biopolymers. 1992;32(2):189-95.
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).