The alpha-helix folds more rapidly at the C-terminus than at the N-terminus

Angela Pozo Ramajo; Sarah A Petty; Agnieszka Starzyk; Sean M Decatur; Martin Volk

doi:10.1021/ja054500+

The alpha-helix folds more rapidly at the C-terminus than at the N-terminus

J Am Chem Soc. 2005 Oct 12;127(40):13784-5. doi: 10.1021/ja054500+.

Authors

Angela Pozo Ramajo¹, Sarah A Petty, Agnieszka Starzyk, Sean M Decatur, Martin Volk

Affiliation

¹ Department of Chemistry and Surface Science Research Centre, University of Liverpool, Liverpool L69 3BX, UK.

PMID: 16201787
DOI: 10.1021/ja054500+

Abstract

The helix-coil dynamics of different sections of an alpha-helical model peptide were observed separately by nanosecond temperature jump experiments with IR detection on a series of isotopically labeled peptides. The results show that the helix-coil dynamics of the alpha-helical C-terminus are faster than those of the N-terminus.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Peptides / chemistry*
Protein Folding*
Protein Structure, Secondary
Temperature
Time Factors

Substances

Peptides