Linked Life Data

17206630

Source:http://linkedlifedata.com/resource/pubmed/id/17206630

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-4-30
pubmed:abstractText
Although the structural analysis of membrane proteins is advancing, an understanding of the basic principles that underlie their folding and assembly remains limited because of the high insolubility intrinsic to these molecules and concomitant challenges in obtaining crystals. Fortunately, from an experimental standpoint, membrane protein folding can be approximated as the rigid-body docking of pre-formed alpha-helical transmembrane segments one with another to form the final functional protein structure. Peptides derived from the sequences of native alpha-helical transmembrane segments and those that mimic their properties are therefore valuable in the experimental evaluation of protein folding within the membrane. Here we present an overview of the progress made in our laboratory and elsewhere in using peptide models toward defining the sequence requirements and forces stabilizing membrane protein folds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
217-32
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Peptides as transmembrane segments: decrypting the determinants for helix-helix interactions in membrane proteins.
pubmed:affiliation
Division of Molecular Structure and Function, Research Institute, Hospital for Sick Children, Toronto, Ont, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't