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Contribution of dipole-dipole interactions to the stability of the collagen triple helix (44 views)

Improta R, Berisio R, Vitagliano L

Protein Sci Protein Science (ISSN: 0961-8368), 2008 May; 17(5): 955-961.

Abstract
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.

Affiliations ▼
*** IBB - CNR Affiliation

Istituto di Biostrutture e Bioimmagini, CNR, I-80134 Napoli, Italy

Details ▼
Impact factor: 3.115, 5-year impact factor: 3.484

Paper type: Journal Article,

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,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-43049098250&partnerID=40&md5=f5455e8b3243c6c6793dab5e71d95357

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Jenkins, C. L., Raines, R. T., Insights on the conformational stability of collagen (2002) Nat. Prod. Rep, 19, pp. 49-59

Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967

Rucker, A. L., Pager, C. T., Campbell, M. N., Qualls, J. E., Creamer, T. P., Host-guest scale of left-handed polyproline II helix formation (2003) Proteins, 53, pp. 68-75

Tsuzuki, S., L thi, H. P., Interaction energies of van der Waals and hydrogen bonded systems calculated using density functional theory: Assessing the PW91 model (2001) J. Chem. Phys, 114, pp. 3949-3957

Wesolowski, T. A., Parisel, O., Ellinger, Y., Weber, J., Comparative study of benzene X (X = O2, N2, CO) complexes using density functional theory: The importance of an accurate exchange-correlation energy density at high reduced density gradients (1997) J. Phys. Chem, 101, pp. 7818-7825


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* Role of side chains in collagen triple helix stabilization and partner recognition (76 views)
Berisio R, De Simone A, Ruggiero A, Improta R, Vitagliano L
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 131-140.

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1 Records (1 excluding Abstracts and Conferences).
Total impact factor: 1.807 (1.807 excluding Abstracts and Conferences).
Total 5-year impact factor: 1.872 (1.872 excluding Abstracts and Conferences).



Your bibliography query: (([btitle, keywords, abstract] COLLAGEN AND [btitle, keywords, abstract] IMINO AND [btitle, keywords, abstract] ACIDS AND [btitle, keywords, abstract] PROTEIN AND [btitle, keywords, abstract] ASSOCIATION)) AND NOT [id] = 9150



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