Sequence dependence of renucleation after a Gly mutation in model collagen peptides.

Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Research Abstract Details 

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Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Abstract Text:

Timothy J Hyde,Michael A Bryan,Barbara Brodsky,Jean Baum,

Missense mutations in the collagen triple helix that replace one Gly residue in the (Gly-X-Y)(n) repeating pattern by a larger amino acid have been shown to delay triple helix folding. One hypothesis is that such mutations interfere with the C- to N-terminal directional propagation and that the identity of the residues immediately N-terminal to the mutation site may determine the delay time and the degree of clinical severity. Model peptides are designed to clarify the role of tripeptide sequences N-terminal to the mutation site, with respect to length, stability, and nucleation propensity, to complete triple helix folding. Two sets of peptides with different N-terminal sequences, one with the natural sequence alpha1(I) 886-900, which is just adjacent to the Gly(901) mutation, and one with a GPO(GAO)(3) sequence, which occurs at alpha1(I) 865-879, are studied by CD and NMR. Placement of the five tripeptides of the natural alpha1(I) collagen sequence N-terminal to the Gly to Ala mutation site results in a peptide that is folded only C-terminal to the mutation site. In contrast, the presence of the Hyp-rich sequence GPO(GAO)(3) N-terminal to the mutation allows complete refolding in the presence of the mutation. The completely folded peptide contains an ordered central region with unusual hydrogen bonding while maintaining standard triple helix structure at the N- and C-terminal ends. These peptide results suggest that the location and sequences of downstream regions favorable for renucleation could be the key factor in the completion of a triple helix N-terminal to a mutation.

Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Publishing Authors By Initials

TJ Hyde,MA Bryan,B Brodsky,J Baum,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

PUBMED ID PMID:

MEDLINE DATE:

Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 36937-43

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 22

MONTH: 09

YEAR: 2006

Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Keywords Mesh Terms:

KEYWORDS: Sequence Homology, Amino Acid

MESH TERMS: chemistry

Chemical & Substance for Abstract: Sequence dependence of renucleation after a Gly mutation in model collagen peptides. Information

Substance Name: Collagen

Registry Number: 9007-34-5

Grant and Affiliation Information for Sequence dependence of renucleation after a Gly mutation in model collagen peptides.

AFFILIATION: Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM60048

ACRONYM: GM

MEDLINETA: J Biol Chem

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