Linked Life Data

20536133

Source:http://linkedlifedata.com/resource/pubmed/id/20536133

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
2010-6-30
pubmed:abstractText
We describe the first example of the recursive selection of biologically relevant macromolecules from a dynamic combinatorial library (DCL). A small library of 36 peptides was allowed to undergo self-association in aqueous solution to form 8436 trimers. The stability of each of these trimers was governed by the formation of a well-packed hydrophobic core. The DCL allowed variation of the hydrophobic residues comprising this core over all combinations of glycine, alanine, valine, leucine, isoleucine, and phenylalanine at six positions. The study leads to three important conclusions: (i) fewer than 0.2% of all possible core packing arrangements have high folding stabilities; (ii) these arrangements are stabilized by intimate "jigsaw" packing, not by sequestration of maximum hydrophobic surface area; (iii) a well-defined "rule" for packing of stable cores exists, but this rule is nuanced by the presence of two unexpected amino acid sequences and the absence of one expected amino acid sequence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8894-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Protein core packing by dynamic combinatorial chemistry.
pubmed:affiliation
Department of Chemistry, The University of Vermont, Burlington, Vermont 05405, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.