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Measuring the refolding of β-sheets with different turn sequences on a nanosecond time scale

Chen, Rita P.-Y. and Huang, Joseph J.-T. and Chen, Hsin-Liang and Jan, Howard and Velusamy, Marappan and Lee, Chung-Tien and Fann, Wunshain and Larsen, Randy W. and Chan, Sunney I. (2004) Measuring the refolding of β-sheets with different turn sequences on a nanosecond time scale. Proceedings of the National Academy of Sciences of the United States of America, 101 (19). pp. 7305-7310. ISSN 0027-8424. PMCID PMC409914. http://resolver.caltech.edu/CaltechAUTHORS:CHEpnas04

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Abstract

Whether turns play an active or passive role in protein folding remains a controversial issue at this juncture. Here we use a photolabile cage strategy in combination with laser-flash photolysis and photoacoustic calorimetry to study the effects of different turns on the kinetics of beta-hairpin refolding on a nanosecond time scale. This strategy opens up a temporal window to allow the observation of early kinetic events in the protein refolding process at ambient temperature and pH without interference from any denaturants. Our results provide direct evidence demonstrating that even a one-residue difference in the turn region can change the refolding kinetics of a peptide. This observation suggests an active role for turn formation in directing protein folding.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC409914/PubMed CentralArticle
ORCID:
AuthorORCID
Chan, Sunney I.0000-0002-5348-2723
Additional Information:Copyright © 2004 by the National Academy of Sciences. Edited by William F. DeGrado, University of Pennsylvania School of Medicine, Philadelphia, PA, and approved March 19, 2004 (received for review August 4, 2003). Published online before print May 3, 2004, 10.1073/pnas.0304922101 We thank Prof. Tien-Yau Luh, Dr. Hsian-Rong Tseng, and Dr. Joern Wirsch in the Department of Chemistry at National Taiwan University for assistance in the synthesis of our linker. This work was supported by a program project grant from Academia Sinica as well as by Grant NSC 91-2119-M-001-012 from the National Science Council, Taiwan. This paper was submitted directly (Track II) to the PNAS office.
Funders:
Funding AgencyGrant Number
Academia SinicaUNSPECIFIED
National Science Council (Taipei)NSC 91-2119-M-001-012
Subject Keywords:SHORT LINEAR PEPTIDE, HAIRPIN FORMATION, AQUEOUS-SOLUTION, DESIGNED PEPTIDES, FOLDING DYNAMICS, B1 DOMAIN, PROTEIN, STABILITY, UBIQUITIN, PHOTOLYSIS
PubMed Central ID:PMC409914
Record Number:CaltechAUTHORS:CHEpnas04
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:CHEpnas04
Alternative URL:http://dx.doi.org/10.1073/pnas.0304922101
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1125
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:21 Dec 2005
Last Modified:22 Sep 2017 04:25

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