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

Rita P.-Y. Chen  , Joseph J.-T. Huang  , Hsin-Liang Chen ^¶ ||, Howard Jan , Marappan Velusamy , Chung-Tien Lee , Wunshain Fann ^¶ ||, Randy W. Larsen , and Sunney I. Chan   

Institutes of Chemistry and ^¶Atomic and Molecular Sciences, Academia Sinica, Taipei 115, Taiwan, Republic of China; Departments of Chemistry and ^||Physics, National Taiwan University, Taipei 106, Taiwan, Republic of China; and Department of Chemistry, University of South Florida, Tampa, FL 33620-5250

Edited by William F. DeGrado, University of Pennsylvania School of Medicine, Philadelphia, PA, and approved March 19, 2004 (received for review August 4, 2003)

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 -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.

Abbreviations: TOCSY, total correlation spectroscopy; MALDI, matrix-assisted laser desorption ionization; E12C, peptide with E-12 to C mutation; c-E12C, cyclized E12C peptide; P6D, peptide with DP-6 to D mutation; P6DE12C, peptide with DP-6 to D and E-12 to C mutations; c-P6DE12C, cyclized P6DE12C peptide.

Present address: Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, Republic of China.

To whom correspondence should be addressed. E-mail: chans{at}chem.sinica.edu.tw .

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