Details

Autor(en) / Beteiligte

• Sabine Frank
• Sergei Boudko
• Kazunori Mizuno
• Therese Schulthess
• Jürgen Engel
• Hans Peter Bächinger

Titel

Collagen Triple Helix Formation Can Be Nucleated at Either End

Ist Teil von

• The Journal of biological chemistry, 2003-03, Vol.278 (10), p.7747-7750

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

2003

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• The directional dependence of folding rates for rod-like macromolecules such as parallel α-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.