Linked Life Data

9136886

Source:http://linkedlifedata.com/resource/pubmed/id/9136886

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1997-6-3
pubmed:abstractText
A de novo designed 33-residue polypeptide folds as a compact beta-sheet sandwich tetramer in aqueous solution. NMR structural analysis shows that although monomer subunits have the same three-stranded antiparallel beta-sheet fold, two equally populated conformational states are identified. Conformational heterogeneity arises from formation of two distinct dimer folds. Each dimer is formed by continuing the monomer beta-sheet into a six-stranded sheet similar to that found in alpha-chemokines. Dimer heterogeneity arises primarily from a two-residue shift in the alignment of interfacial strands. NOE-based conformational modeling has yielded well-defined structures for both dimer types. While the tetramer beta-sheet sandwich most probably results from association of hydrophobic surfaces from two amphipathic dimers, dimers could combine to form either two types of homotetramers and/or one heterotetramer composed of both dimer types. Even though interdimer NOEs could not be unambiguously identified to resolve this point, thermodynamic arguments based on observation of equal populations of both dimer types favor formation of heterotetramers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5245-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
NMR structure of a de novo designed, peptide 33mer with two distinct, compact beta-sheet folds.
pubmed:affiliation
Department of Biochemistry, University of Minnesota Health Sciences Center, Minneapolis 55455, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't