Unknown

Dataset Information

0

A one-dimensional free energy surface does not account for two-probe folding kinetics of protein alpha(3)D.


ABSTRACT: We present fluorescence-detected measurements of the temperature-jump relaxation kinetics of the designed three-helix bundle protein alpha(3)D taken under solvent conditions identical to previous infrared-detected kinetics. The fluorescence-detected rate is similar to the IR-detected rate only at the lowest temperature where we could measure it (326 K). The fluorescence-detected rate decreases by a factor of 3 over the 326-344 K temperature range, whereas the IR-detected rate remains nearly constant over the same range. To investigate this probe dependence, we tested an extensive set of physically reasonable one-dimensional (1D) free energy surfaces by Langevin dynamics simulation. The simulations included coordinate- and temperature-dependent roughness, diffusion coefficients, and IR/fluorescence spectroscopic signatures. None of these can reproduce the IR and fluorescence data simultaneously, forcing us to the conclusion that a 1D free energy surface cannot accurately describe the folding of alpha(3)D. This supports the hypothesis that alpha(3)D has a multidimensional free energy surface conducive to downhill folding at 326 K, and that it is already an incipient downhill folder with probe-dependent kinetics near its melting point.

SUBMITTER: Liu F 

PROVIDER: S-EPMC2671193 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

A one-dimensional free energy surface does not account for two-probe folding kinetics of protein alpha(3)D.

Liu Feng F   Dumont Charles C   Zhu Yongjin Y   DeGrado William F WF   Gai Feng F   Gruebele Martin M  

The Journal of chemical physics 20090201 6


We present fluorescence-detected measurements of the temperature-jump relaxation kinetics of the designed three-helix bundle protein alpha(3)D taken under solvent conditions identical to previous infrared-detected kinetics. The fluorescence-detected rate is similar to the IR-detected rate only at the lowest temperature where we could measure it (326 K). The fluorescence-detected rate decreases by a factor of 3 over the 326-344 K temperature range, whereas the IR-detected rate remains nearly cons  ...[more]

Similar Datasets

| S-EPMC7889939 | biostudies-literature
| S-EPMC2760970 | biostudies-literature
| S-EPMC9847652 | biostudies-literature
| S-EPMC2736680 | biostudies-literature
| S-EPMC2700257 | biostudies-literature
| S-EPMC1502548 | biostudies-literature
| S-EPMC9202546 | biostudies-literature
| S-EPMC2708030 | biostudies-literature
| S-EPMC2756654 | biostudies-literature
| S-EPMC2366061 | biostudies-literature