Linked Life Data

17073435

Source:http://linkedlifedata.com/resource/pubmed/id/17073435

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2006-10-31
pubmed:abstractText
The alpha-helical hairpin is the fundamental building block of the widespread helix-turn-helix DNA binding motif. With two antiparallel helices connected by a reverse turn, the alpha-helical hairpin structure may be regarded as a "supersecondary structural element" and, therefore, could exhibit rather unique folding properties. So far, the folding mechanism of alpha-helical hairpins has not been studied in detail and remains elusive. Herein, we examine the effects of the turn, the hydrophobic cluster, and a disulfide cross-linker on the folding kinetics of a designed alpha-helical hairpin, Z34C, using an infrared temperature-jump (T-jump) method in conjunction with site-specific mutagenesis. Our results show that Z34C folds with an ultrafast rate ( approximately 4.0 x 10(5) s(-1)) and support a folding mechanism in which the rate-limiting step corresponds to the formation of the reverse turn. On the other hand, the hydrophobic cluster and the disulfide cross-linker appear to largely stabilize the native state but not the folding transition state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13131-9
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Understanding the folding mechanism of an alpha-helical hairpin.
pubmed:affiliation
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.