Ruggedness in the Folding Landscape of Protein L

Overview

Journal HFSP J

Specialty Biology

Date 2009 May 14

PMID 19436489

Citations 11

Authors

Steven A Waldauer

Olgica Bakajin

Terry Ball

Yujie Chen

Stephen J DeCamp

Michaela Kopka

Marcus Jager

Vijay R Singh

William J Wedemeyer

Shimon Weiss

Shuhuai Yao

Lisa J Lapidus

Affiliations

Soon will be listed here.

Abstract

By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rapid kinetic experiments, we have found its unfolded state to be more complex than suggested by two-state folding models. Using an ultrarapid mixer to initiate protein folding within approximately 2-4 microseconds, we observe folding kinetics by intrinsic tryptophan fluorescence and fluorescence resonance energy transfer. We detect at least two processes faster than 100 mus that would be hidden within the burst phase of a stopped-flow instrument measuring tryptophan fluorescence. Previously reported measurements of slow intramolecular diffusion are commensurate with the slower of the two observed fast phases. These results suggest that a multidimensional energy landscape is necessary to describe the folding of protein L, and that the dynamics of the unfolded state is dominated by multiple small energy barriers.

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