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Titolo:
STRUCTURE OF THE TYPE-I COLLAGEN MOLECULE BASED ON CONFORMATIONAL ENERGY COMPUTATIONS - THE TRIPLE-STRANDED HELIX AND THE N-TERMINAL TELOPEPTIDE
Autore:
VITAGLIANO L; NEMETHY G; ZAGARI A; SCHERAGA HA;
Indirizzi:
CORNELL UNIV,BAKER LAB CHEM ITHACA NY 14853 CORNELL UNIV,BAKER LAB CHEM ITHACA NY 14853 CNR,CTR STUDIO BIOCRISTALLOG I-80134 NAPLES ITALY UNIV NAPLES,DIPARTIMENTO CHIM I-80134 NAPLES ITALY CUNY MT SINAI SCH MED,DEPT BIOMATH SCI NEW YORK NY 10029
Titolo Testata:
Journal of Molecular Biology
fascicolo: 1, volume: 247, anno: 1995,
pagine: 69 - 80
SICI:
0022-2836(1995)247:1<69:SOTTCM>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; DIFFRACTION PATTERN; NEUTRON-DIFFRACTION; SECONDARY-STRUCTURE; GLOBULAR PROTEINS; NMR-SPECTROSCOPY; ALPHA-2 CHAIN; CROSS-LINKING; PREDICTION; FIBRILS;
Keywords:
COLLAGEN; TELOPEPTIDE; CONFORMATIONAL ANALYSIS; ECEPP (EMPIRICAL CONFORMATIONAL ENERGY PROGRAM FOR PEPTIDES); FOLDING PATHWAYS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
L. Vitagliano et al., "STRUCTURE OF THE TYPE-I COLLAGEN MOLECULE BASED ON CONFORMATIONAL ENERGY COMPUTATIONS - THE TRIPLE-STRANDED HELIX AND THE N-TERMINAL TELOPEPTIDE", Journal of Molecular Biology, 247(1), 1995, pp. 69-80

Abstract

Various studies have implicated a crucial role for the non-helical ends (telopeptides) of the collagen molecule during fibrillogenesis. In this paper, the first extensive conformational analysis of the type I collagen N-terminal telopeptide is reported. The commonly used ''build-up'' procedure for peptides and proteins has been used, with relevantmodifications to take account of all the stereochemical constraints affecting the telopeptide. In particular, consideration was given not only to the interactions among the three chains that constitute the telopeptide, but also to the interactions between the telopeptide and thecovalently linked triple helix. The computations led to a limited number of different structures within an energy range of 25 kcal/mol. Comparison of these models clearly shows that the portion of the telopeptide linked to the triple helix is rather rigid whereas its N terminus is more flexible. Furthermore, the lowest-energy structure has an energy that is markedly lower (by 7.75 kcal/mol) than that of other conformations with different structural features. The lowest-energy model ofthe N-terminal telopeptide, which differs from previous proposed models, has a contracted conformation compared to the triple helix region,in agreement with X-ray and neutron diffraction data on collagen fibers. Finally, the side-chains of the lysine residues of the telopeptide, involved in intermolecular cross-links in mature collagen fibers, are oriented to protrude to the exterior, in positions to interact with adjacent collagen molecules.

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Documento generato il 14/07/20 alle ore 11:43:15