Biopolym. Cell. 2006; 22(6):458-467.
http://dx.doi.org/10.7124/bc.00074D
Молекулярна біофізика
Фізичні фактори стабільності трьохспіральних структур колагенового типу
1Борискіна О. П., 1Больбух Т. В., 1Семенов М. О., 1Малєєв В. Я.
  1. Інститут радіофізики і електроніки ім. А. Я. Усикова НАН України
    вул. Академіка Проскури, 12, Харків, Україна, 61085

Abstract

Розраховано ентальпію міжпептидних водневих зв'язків та енергію гідратації модельного колагенового політрипептиду poly (Gly-Pro-Pro) та колагену, а також оцінено відносні внески енергій різних типів взаємодій у загальну енергію стабілізації трьохспіральних структур колагенового типу. Розрахунок здійснено на основі даних комплексу експериментальних фі­зичних методик: 14 спектроскопії, пьєзогравіметрії та диференційної сканувальної калориметрії.
Keywords: колаген, poly(Gly-Pro-Pro), енергія гідра­ тації, ентальпія водневих зв'язків, ІЧ спектроскопія
Повний текст: (PDF, російською) (PDF, англійською)

References

[1] Ramshaw JA, Shah NK, Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J Struct Biol. 1998;122(1-2):86-91.
[2] Nikitin VN, Perskiy EE, Utevskaya LA. Developmental and evolutionary biochemistry of collagen structures. K: Naukova Dumka. 1977; 279 p.
[3] Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple-helical structure. Nat Struct Biol. 1999;6(5):454-7.
[4] Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin alpha2beta1. Cell. 2000;101(1):47-56.
[5] Berisio R, Vitagliano L, Mazzarella L, Zagari A. Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3). Protein Sci. 2002;11(2):262-70.
[6] Berisio R, Vitagliano L, Mazzarella L, Zagari A. Crystal structure of a collagen-like polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 A resolution: implications for collagen hydration. Biopolymers. 2000-2001;56(1):8-13.
[7] Rainey JK, Goh MC. A statistically derived parameterization for the collagen triple-helix. Protein Sci. 2002;11(11):2748-54.
[8] Pineri MH, Escoubes M, Roche G. Water--collagen interactions: calorimetric and mechanical experiments. Biopolymers. 1978;17(12):2799-2815.
[9] Eisenmenger F, Eisenhaber F, Tumanyan VG, Esipova NG. Monte Carlo simulation of the water environment of collagen. Stud Biophys. 1983; 98:155-60.
[10] 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.
[11] Privalov PL. Stability of proteins. Proteins which do not present a single cooperative system. Adv Protein Chem. 1982;35:1-104.
[12] Engel J, Chen HT, Prockop DJ, Klump H. The triple helix in equilibrium with coil conversion of collagen-like polytripeptides in aqueous and nonaqueous 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(3):601-22.
[13] Holmgren SK, Taylor KM, Bretscher LE, Raines RT. Code for collagen's stability deciphered. Nature. 1998;392(6677):666-7.
[14] Jenkins CL, Raines RT. Insights on the conformational stability of collagen. Nat Prod Rep. 2002;19(1):49-59.
[15] Tumanyan VG, Esipova NG. Comprehensive conformational analysis of (Gly-Pro-Pro)n and (Gly-Pro-Hyp)n related to collagen. Biopolymers. 1982;21(3):475-97.
[16] Lazarev YA, Lobachov VM, Grishkovski BA, Shibnev VA, Grechishko VS, Finogenova MP, Esipova NG, Rogulenkova VN. Formation of the collagen-like triple-helical structure in oligopeptides during elongation of the molecular chain. Biopolymers. 1978;17(5):1215-33.
[17] Bella J, Eaton M, Brodsky B, Berman HM. Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science. 1994;266(5182):75-81.
[18] Miles CA, Ghelashvili M. Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers. Biophys J. 1999;76(6):3243-52.
[19] Traub W, Yonath A. Polymers of tripeptides as collagen models. I. X-ray studies of poly(L-prolyl-glycyl-L-proline) and related polytripeptides. J Mol Biol. 1966;16(2):404-14.
[20] Semenov M, Bolbukh T, Maleev V. Infrared study of the influence of water on DNA stability in the dependence on AT/GC composition. J Mol Struct. 1997;408-409:213–7.
[21] Semenov MA, Bereznhyak EG. Hydration and stability of nucleic acids in the condensed state. Comments Mol Cel Biophys. 2000; 10: 1-23.
[22] Chandrakasan G, Torchia DA, Piez KA. Preparation of intact monomeric collagen from rat tail tendon and skin and the structure of the nonhelical ends in solution. J Biol Chem. 1976;251(19):6062-7.
[23] Wexler A, Hasegawa S. Relative humidity-temperature relationships of some saturated salt solutions in the temperature range 0 degree to 50 degrees C. J Res Natl Bur Stand. 1954;53(1):19-26.
[24] Lazarev YA, Grishkovsky BA, Khromova TB. Amide I band of IR spectrum and structure of collagen and related polypeptides. Biopolymers. 1985;24(8):1449-78.
[25] Semenov MA, Starikov EB, Bolbukh TV. Hydration isotherms and structural state of nucleotides and polynuc­ leotides. Stud biophys. 1988; 123: 217-224.
[26] Gasan AI, Maleev VYa, Semenov MA. Role of water in stabilizing the helical biomacromolecules DNA and collagen. Stud biophys. 1990.; 136:171-8.
[27] Falk M, Hartman KA, Lord RC. Hydration of Deoxyribonucleic Acid. I. a Gravimetric Study . J Am Chem Soc. 1962;84(20):3843–6.
[28] Buck M, Karplus M. Hydrogen Bond Energetics: A Simulation and Statistical Analysis of N -Methyl Acetamide (NMA), Water, and Human Lysozyme. J Phys Chem. 2001;105(44):11000–15.
[29] Miyazawa T, Blout ER. The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands 1 . J Am Chem Soc. 1961;83(3):712–9.
[30] Chirgadza YuN. Infrared spectra and structure of polypeptides and proteins. M.: Nauka, 1965. 135 p.
[31] Traub W, Yonath A. Polymers of tripeptides as collagen models. I. X-ray studies of poly(L-prolyl-glycyl-L-proline) and related polytripeptides. J Mol Biol. 1966;16(2):404-14.
[32] Gordon PL, Huang C, Lord RC, Yannas IV. The far-infrared spectrum of collagen. Macromolecules. 1974;7(6):954-6.
[33] Melezhik EP, Semenov MA. Resonant interaction of carbonyl vibrations in the collagen structure. Biofiz Visn. 2003; 606(13):62-8.
[34] Melezhik EP, Semenov MA, Ivanov AYu.ne structure of the amide I band FT-IR spectrum of collagen. Biofiz Visn. 2005; 665(15): 62-7.
[35] Semenov MA. Hydration and structural condition of the nucleic acids in the condensed state: Thesis. ... dr fiz-mat. nauk. M.: MGU, 1990.
[36] Schellman JA. The stability of hydrogen-bonded peptide structures in aqueous solution. C r Trav Lab Carlsberg Ser. Chim. 1955; 29: 230-259.
[37] Radmer RJ, Klein TE. Triple helical structure and stabilization of collagen-like molecules with 4(R)-hydroxyproline in the Xaa position. Biophys J. 2006;90(2):578-88.
[38] Maleev VY, Gasan AI. A statistical mechanical study of helix-coil transition in concentrated solutions of polypeptides and proteins. Biopolymers. 1974;13(12):2409-22.