Contribution of dipole-dipole interactions to the stability of the collagen triple helix (639 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2008 May; 17(5): 955-961.
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Paper type: Journal Article,
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Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-43049098250&partnerID=40&md5=f5455e8b3243c6c6793dab5e71d95357
Keywords: Collagen, Imino Acids, Protein-Protein Association, Quantum Chemistry, Triple Helix, Glycine, Hydroxyproline, Article, Dipole, Priority Journal, Protein Motif, Protein Stability, Protein Structure, Structure Analysis, X Ray Analysis, Amino Acid Motifs, Animals, Crystallography, X-Ray, Humans, Peptides,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, I-80134 Napoli, Italy
References:
Not available.
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2008 May; 17(5): 955-961.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.115, 5-year impact factor: 3.484
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-43049098250&partnerID=40&md5=f5455e8b3243c6c6793dab5e71d95357
Keywords: Collagen, Imino Acids, Protein-Protein Association, Quantum Chemistry, Triple Helix, Glycine, Hydroxyproline, Article, Dipole, Priority Journal, Protein Motif, Protein Stability, Protein Structure, Structure Analysis, X Ray Analysis, Amino Acid Motifs, Animals, Crystallography, X-Ray, Humans, Peptides,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, I-80134 Napoli, Italy
References:
Not available.
Contribution of dipole-dipole interactions to the stability of the collagen triple helix
Unveiling sequence-stability and structure-stability relationships is a major goal of protein chemistry and structural biology. Despite the enormous efforts devoted, answers to these issues remain elusive. In principle, collagen represents an ideal system for such investigations due to its simplified sequence and regular structure. However, the definition of the molecular basis of collagen triple helix stability has hitherto proved to be a difficult task. Particularly puzzling is the decoding of the mechanism of triple helix stabilization/destabilization induced by imino acids. Although the propensity-based model, which correlates the propensities of the individual imino acids with the structural requirements of the triple helix, is able to explicate most of the experimental data, it is unable to predict the rather high stability of peptides embedding Gly-Hyp-Hyp triplets. Starting from the available X-ray structures of this polypeptide, we carried out an extensive quantum chemistry analysis of the mutual interactions established by hydroxyproline residues located at the X and Y positions of the Gly-X-Y motif. Our data clearly indicate that the opposing rings of these residues establish significant van der Waals and dipole-dipole interactions that play an important role in triple helix stabilization. These findings suggest that triple helix stabilization can be achieved by distinct structural mechanisms. The interplay of these subtle but recurrent effects dictates the overall stability of this widespread structural motif. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society.
Unveiling sequence-stability and structure-stability relationships is a major goal of protein chemistry and structural biology. Despite the enormous efforts devoted, answers to these issues remain elusive. In principle, collagen represents an ideal system for such investigations due to its simplified sequence and regular structure. However, the definition of the molecular basis of collagen triple helix stability has hitherto proved to be a difficult task. Particularly puzzling is the decoding of the mechanism of triple helix stabilization/destabilization induced by imino acids. Although the propensity-based model, which correlates the propensities of the individual imino acids with the structural requirements of the triple helix, is able to explicate most of the experimental data, it is unable to predict the rather high stability of peptides embedding Gly-Hyp-Hyp triplets. Starting from the available X-ray structures of this polypeptide, we carried out an extensive quantum chemistry analysis of the mutual interactions established by hydroxyproline residues located at the X and Y positions of the Gly-X-Y motif. Our data clearly indicate that the opposing rings of these residues establish significant van der Waals and dipole-dipole interactions that play an important role in triple helix stabilization. These findings suggest that triple helix stabilization can be achieved by distinct structural mechanisms. The interplay of these subtle but recurrent effects dictates the overall stability of this widespread structural motif. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society.
Contribution of dipole-dipole interactions to the stability of the collagen triple helix
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Contribution of dipole-dipole interactions to the stability of the collagen triple helix
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Recent progress on collagen triple helix structure, stability and assembly (1030 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116.
Impact Factor: 0.622
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (940 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Impact Factor: 3.546
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Benzi C, Improta R, Scalmani G, Barone V
* Quantum mechanical study of the conformational behavior of proline and 4R-hydroxyproline dipeptide analogues in vacuum and in aqueous solution (494 views)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2002 Feb; 23(3): 341-350.
Impact Factor: 2.931
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Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
* Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (1481 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Impact Factor: 3.472
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Structural bases of collagen stabilization induced by proline hydroxylation (1060 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001 Apr 15; 58(5): 459-464.
Impact Factor: 1.845
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (609 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
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Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (761 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1998 Jul 24; 280(4): 623-638.
Impact Factor: 5.803
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Pavone V, Rossi F, Pucci P, Andini S, Ferrara L, Di Blasio B, Pedone C
Studies on gliadin related peptides. I. Synthesis, purification and 1H n. m. r. characterization of the pentapeptide H-Tyr-(Gln)3-Pro-OH (1083 views)
Int J Pept Protein Res (ISSN: 0367-8377, 0367-8377print), 1983 Oct; 22(4): 482-488.
Impact Factor: 1.255
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34 Records (34 excluding Abstracts).
Total impact factor: 129.379 (129.379 excluding Abstracts).
Total 5 year impact factor: 144.706 (144.706 excluding Abstracts).
Total impact factor: 129.379 (129.379 excluding Abstracts).
Total 5 year impact factor: 144.706 (144.706 excluding Abstracts).
639 views. Last view on Friday 13 December 2024, 22:31:15
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