Linked Life Data

10194328

Source:http://linkedlifedata.com/resource/pubmed/id/10194328

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1999-4-21
pubmed:abstractText
Despite its small size, the peripheral subunit-binding domain from the dihydrolipoamide acetyltransferase component of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex adopts a unique, compact structure. To determine whether the full 43 residue sequence is required for the domain to adopt a stable, nativelike structure, 3 proteins of different lengths were prepared. Psbd41 corresponds to residues 3-43 of the domain, psbd36 spans residues 6-41, and psbd33 comprises residues 7-39. Psbd41 folds in a cooperative, two-state fashion with a Tm of 53 degrees C and a stability at 25 degrees C of 2.2 kcal mol-1. Psbd36 is nearly as stable with a Tm of 48 degrees C and a stability of 1.8 kcal mol-1. Similar m-values and heat capacities suggest that psbd36 and psbd41 bury approximately the same surface area. Minimal differences in CalphaH and NH chemical shifts between psbd41 and psbd36 show that the two sequences adopt the same tertiary fold. On a per residue basis, DeltaH degrees and DeltaC degrees p fall within the range typical for single-domain globular proteins. Psbd33 is significantly less stable. It is not fully folded at 25 degrees C, and at all temperatures it shows broadened NMR lines. ANS titrations provide evidence that this is due to an equilibrium between nativelike and unfolded molecules rather than formation of a molten globule. The fraction of psbd33 molecules which are folded appear to adopt the same structure as the full-length domain. Thus, although more than the 33 residue core is required to form a fully stable native structure, the entire sequence is not required for folding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4128-36
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Nativelike structure and stability in a truncation mutant of a protein minidomain: the peripheral subunit-binding domain.
pubmed:affiliation
Department of Physiology and Biophysics, State University of New York at Stony Brook 11794-8661, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't