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The unfolding and folding dynamics of TNfnALL probed by single molecule force-ramp spectroscopy

TitleThe unfolding and folding dynamics of TNfnALL probed by single molecule force-ramp spectroscopy
Publication TypeJournal Article
Year of Publication2006
AuthorsWang, MJ, Cao, Y, Li, HB
JournalPolymer
Volume47
Pagination2548-2554
Date PublishedMar
Type of ArticleArticle
ISBN Number0032-3861
KeywordsADHESION, DOMAIN, EXPRESSION, III, IMMUNOGLOBULIN, MATRIX PROTEINS, MECHANICAL STABILITY, microscopy, MUSCLE PROTEIN TITIN, tenascin, UBIQUITIN
Abstract

Tenascin, an important extracellular matrix protein, is subject to stretching force under physiological conditions and plays important roles in regulating the cell-matrix interactions. Using the recently developed single molecule force-ramp spectroscopy, we investigated the unfolding-folding kinetics of a recombinant tenascin fragment TNfnALL. Our results showed that all the 15 FnIII domains in TNfnALL have similar spontaneous unfolding rate constant at zero force, but show great difference in their folding rate constants. Our results demonstrated that single molecule force-ramp spectroscopy is a powerful tool for accurate determination of the kinetic parameters that characterize the unfolding and folding reactions. We anticipate that single molecule force-ramp spectroscopy will become a versatile addition to the single molecule manipulation tool box and greatly expand the scope of single molecule force spectroscopy. (c) 2006 Elsevier Ltd. All rights reserved.

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