NDLI: The origins of asymmetry in the folding transition states of protein L and protein G

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The origins of asymmetry in the folding transition states of protein L and protein G

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Brooks, Charles L. Karanicolas, John
Description	Country affiliation: United States Author Affiliation: Karanicolas J ( Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.)
Abstract	Topology has been shown to be an important determinant of many features of protein folding; however, the delineation of sequence effects on folding remains obscure. Furthermore, differentiation between the two influences proves difficult due to their intimate relationship. To investigate the effect of sequence in the absence of significant topological differences, we examined the folding mechanisms of segment B1 peptostreptococcal protein L and segment B1 of streptococcal protein G. These proteins share the same highly symmetrical topology. Despite this symmetry, neither protein folds through a symmetrical transition state. We analyzed the origins of this difference using theoretical models. We found that the strength of the interactions present in the N-terminal hairpin of protein L causes this hairpin to form ahead of the C-terminal hairpin. The difference in chain entropy associated with the formation of the hairpins of protein G proves sufficient to beget initiation of folding at the shorter C-terminal hairpin. Our findings suggest that the mechanism of folding may be understood by examination of the free energy associated with the formation of partially folded microstates.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	10
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Dna-binding Proteins Metabolism Nerve Tissue Proteins Protein Folding Algorithms Computational Biology Models, Molecular Protein Structure, Tertiary Physiology Thermodynamics Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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