Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 338, Issue 3, Pages 445-451Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2004.02.062
Keywords
protein folding; titin; multiple pathways; transition state; temperature dependence
Categories
Ask authors/readers for more resources
Recent work has shown that a beta-sandwich domain from the human muscle protein titin (TI I27) unfolds via more than one pathway, providing experimental evidence for a long-standing theoretical prediction in protein folding. Here we present a thermodynamic analysis of two transition states along different folding pathways for this protein. The unusual unfolding kinetics is increased at both high and low temperatures, indicating that the high denaturant pathway is becoming more accessible. The transition states in each pathway are structurally distinct and have very different heat capacities. Interestingly the nucleation-condensation pathway is dominant at all physiologically relevant temperatures, supporting the suggestion that pathways with diffuse rather than localised transition states have been selected for by evolution to prevent misfolding. (C) 2004 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available