Thermodynamics of Formation of the Triple Helix from Free Chains and from Template-Constrained Chains of Collagen-like Monodisperse Poly(Gly-Pro-Hyp) Structures
Statistical thermodynamic methods, developed for treating the α-helix−coil transition, are applied herein to describe the formation of the triple helix from short free chains and short template-constrained chains of collagen-like monodisperse poly(tripeptides), using poly(Gly-Pro-Hyp) as the example...
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Published in: | The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment, & general theory Vol. 103; no. 49; pp. 10561 - 10566 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
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American Chemical Society
09-12-1999
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Abstract | Statistical thermodynamic methods, developed for treating the α-helix−coil transition, are applied herein to describe the formation of the triple helix from short free chains and short template-constrained chains of collagen-like monodisperse poly(tripeptides), using poly(Gly-Pro-Hyp) as the example. For such short chains, application of the one-helical-sequence approximation indicates that there is very little unwinding from the ends, so that an all-or-none model is adequate to treat this transition. From the dependence of the helix nucleation and propagation parameters on chain length, concentration, and temperature, the thermodynamic parameters for formation of the triple helix from both free chains and template-constrained monodisperse poly(Gly-Pro-Hyp) chains are similar, and also similar to those for free poly(Gly-Pro-Pro) chains. |
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AbstractList | Statistical thermodynamic methods, developed for treating the α-helix−coil transition, are applied herein to describe the formation of the triple helix from short free chains and short template-constrained chains of collagen-like monodisperse poly(tripeptides), using poly(Gly-Pro-Hyp) as the example. For such short chains, application of the one-helical-sequence approximation indicates that there is very little unwinding from the ends, so that an all-or-none model is adequate to treat this transition. From the dependence of the helix nucleation and propagation parameters on chain length, concentration, and temperature, the thermodynamic parameters for formation of the triple helix from both free chains and template-constrained monodisperse poly(Gly-Pro-Hyp) chains are similar, and also similar to those for free poly(Gly-Pro-Pro) chains. |
Author | Scheraga, Harold A Goodman, Murray Locardi, Elsa Kwak, Juliann |
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CitedBy_id | crossref_primary_10_1074_jbc_M605236200 crossref_primary_10_3390_sym12111926 crossref_primary_10_1021_jp0625715 crossref_primary_10_1021_ma202176w crossref_primary_10_1021_jp212631q crossref_primary_10_1021_bi015952b crossref_primary_10_1016_j_theochem_2007_11_030 crossref_primary_10_1021_jp070266t crossref_primary_10_1021_jp805979k |
Cites_doi | 10.1063/1.1674701 10.1002/bip.1974.360130916 10.1021/ja01502a018 10.1002/bip.1974.360130917 10.1021/bi00821a010 10.1021/ja961260c 10.1002/bip.1974.360130405 10.1021/ma60022a008 10.1002/bip.1973.360120818 10.1021/ja9612615 10.1002/bip.360280907 10.1002/bip.1980.360191017 |
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References | Feng Y. Ph.D. (jp9925435b00014/jp9925435b00014_1) 1996 Poland D. (jp9925435b00011/jp9925435b00011_1) 1970 Nemethy G. (jp9925435b00008/jp9925435b00008_1) 1989; 28 Schwarz M. (jp9925435b00004/jp9925435b00004_1) 1974; 13 Harrington W. F. (jp9925435b00002/jp9925435b00002_1) 1970; 9 Gõ N. (jp9925435b00003/jp9925435b00003_1) 1973; 12 Von Dreele P. H. (jp9925435b00013/jp9925435b00013_1) 1971; 4 Gõ M. (jp9925435b00012/jp9925435b00012_1) 1971; 54 Feng Y. (jp9925435b00009/jp9925435b00009_1) 1996; 118 Flory P. J. (jp9925435b00001/jp9925435b00001_1) 1960; 82 Roth W. (jp9925435b00007/jp9925435b00007_1) 1980; 19 Melacini G. (jp9925435b00010/jp9925435b00010_1) 1996; 118 Schwarz M. (jp9925435b00006/jp9925435b00006_1) 1974; 13 Poland D. (jp9925435b00005/jp9925435b00005_1) 1974; 13 |
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Title | Thermodynamics of Formation of the Triple Helix from Free Chains and from Template-Constrained Chains of Collagen-like Monodisperse Poly(Gly-Pro-Hyp) Structures |
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