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Journal article

Collagen triple helix formation can be nucleated at either end.

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  • 2003-01-24
Published in:
  • The Journal of biological chemistry. - 2003
Amino Acid Sequence
Collagen
Kinetics
Mass Spectrometry
Molecular Sequence Data
Protein Conformation
Protein Denaturation
Protein Folding
Recombinant Proteins
Ultracentrifugation
English The directional dependence of folding rates for rod-like macromolecules such as parallel alpha-helical coiled-coils, DNA double-helices, and collagen triple helices is largely unexplored. This is mainly due to technical difficulties in measuring rates in different directions. Folding of collagens is nucleated by trimeric non-collagenous domains. These are usually located at the COOH terminus, suggesting that triple helix folding proceeds from the COOH to the NH(2) terminus. Evidence is presented here that effective nucleation is possible at both ends of the collagen-like peptide (Gly-Pro-Pro)(10), using designed proteins in which this peptide is fused either NH(2)- or COOH-terminal to a nucleation domain, either T4-phage foldon or the disulfide knot of type III collagen. The location of the nucleation domain influences triple-helical stability, which might be explained by differences in the linker sequences and the presence or absence of repulsive charges at the carboxyl-terminal end of the triple helix. Triple helical folding rates are found to be independent of the site of nucleation and consistent with cis-trans isomerization being the rate-limiting step.
Language
  • English
Open access status
bronze
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Persistent URL
https://sonar.rero.ch/global/documents/288226
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