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Comparative NMR analysis of collagen triple helix organization from N- to C-termini

Comparative NMR analysis of collagen triple helix organization from N- to C-termini
Comparative NMR analysis of collagen triple helix organization from N- to C-termini
The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by dry weight it is the most abundant fold in mammalian tissues. Many factors affecting the structure and stability of collagen have been determined through the use of short synthetically prepared peptides, generally called collagen-mimetic peptides (CMPs). NMR (nuclear magnetic resonance spectroscopy) investigations into the molecular structure of CMPs have suffered from large amounts of signal overlap and degeneracy because of collagen’s repetitive primary sequence, the close and symmetric packing of the three chains and the identical peptide sequences found in homotrimers. In this paper a peptide library is prepared in which a single isotopic 15N-Gly label is moved sequentially along the peptide backbone. Our approach allows for a more explicit examination of local topology than available in past reports. This reveals larger regions of disorder at the C-terminus than previously detected by crystallographic or NMR studies, and here C-terminal fraying is seen to extend for six amino acids in a (POG)10 sequence. Furthermore, small sequence changes at the N-terminus greatly influence the degree of this localized disorder and may be useful in the future design of CMPs to maximize collagen’s interstrand hydrogen bonding pattern. Our approach and data serves as a reference for future CMP characterizations to determine the quality and extent of folding.
1525-7797
145-155
Acevedo-jake, Amanda M.
648b12e3-763b-4e0b-bf33-abf4f85be1ef
Jalan, Abhishek A.
12c5f601-866c-4a3c-b819-4ab2fea64921
Hartgerink, Jeffrey D.
37f5e1c8-1280-4133-8584-b327d6fcaaeb
Acevedo-jake, Amanda M.
648b12e3-763b-4e0b-bf33-abf4f85be1ef
Jalan, Abhishek A.
12c5f601-866c-4a3c-b819-4ab2fea64921
Hartgerink, Jeffrey D.
37f5e1c8-1280-4133-8584-b327d6fcaaeb

Acevedo-jake, Amanda M., Jalan, Abhishek A. and Hartgerink, Jeffrey D. (2014) Comparative NMR analysis of collagen triple helix organization from N- to C-termini. Biomacromolecules, 16 (1), 145-155. (doi:10.1021/bm501281a).

Record type: Article

Abstract

The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by dry weight it is the most abundant fold in mammalian tissues. Many factors affecting the structure and stability of collagen have been determined through the use of short synthetically prepared peptides, generally called collagen-mimetic peptides (CMPs). NMR (nuclear magnetic resonance spectroscopy) investigations into the molecular structure of CMPs have suffered from large amounts of signal overlap and degeneracy because of collagen’s repetitive primary sequence, the close and symmetric packing of the three chains and the identical peptide sequences found in homotrimers. In this paper a peptide library is prepared in which a single isotopic 15N-Gly label is moved sequentially along the peptide backbone. Our approach allows for a more explicit examination of local topology than available in past reports. This reveals larger regions of disorder at the C-terminus than previously detected by crystallographic or NMR studies, and here C-terminal fraying is seen to extend for six amino acids in a (POG)10 sequence. Furthermore, small sequence changes at the N-terminus greatly influence the degree of this localized disorder and may be useful in the future design of CMPs to maximize collagen’s interstrand hydrogen bonding pattern. Our approach and data serves as a reference for future CMP characterizations to determine the quality and extent of folding.

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Published date: 10 December 2014

Identifiers

Local EPrints ID: 434522
URI: http://eprints.soton.ac.uk/id/eprint/434522
ISSN: 1525-7797
PURE UUID: 99898437-59b1-4c3f-9bbd-3de70c0b6cce

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Date deposited: 26 Sep 2019 16:30
Last modified: 26 Sep 2019 16:30

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Contributors

Author: Amanda M. Acevedo-jake
Author: Abhishek A. Jalan
Author: Jeffrey D. Hartgerink

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