Linked Life Data

15504411

Source:http://linkedlifedata.com/resource/pubmed/id/15504411

Statements in which the resource exists.
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pubmed-article:15504411pubmed:abstractTextThe study of proteins with the same architecture, but different sequence has proven to be a valuable tool in the protein folding field. As a prelude to studies on the folding mechanism of spectrin domains we present the kinetic characterisation of the wild-type forms of the 15th, 16th, and 17th domains of chicken brain alpha-spectrin (referred to as R15, R16 and R17, respectively). We show that the proteins all behave in a two-state manner, with different kinetic properties. The folding rate varies remarkably between different members, with a 5000-fold variation in folding rate and 3000-fold variation in unfolding rate seen for proteins differing only 1 kcal mol(-1) in stability. We show clear evidence for significant complexity in the energy landscape of R16, which shows a change in amplitude outside the stopped-flow timescale and curvature in the unfolding arm of the chevron plot. The accompanying paper describes the characterisation of the folding pathway of this domain.lld:pubmed
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pubmed-article:15504411pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15504411pubmed:year2004lld:pubmed
pubmed-article:15504411pubmed:articleTitleThe folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties.lld:pubmed
pubmed-article:15504411pubmed:affiliationMRC Centre for Protein Engineering, University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK.lld:pubmed
pubmed-article:15504411pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15504411pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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