Linked Life Data

11148022

Source:http://linkedlifedata.com/resource/pubmed/id/11148022

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-1-23
pubmed:abstractText
Isolating spacers introduced between solubilizing lysine regions and a polyalanine core permit rigorous characterization of context-free alanine helices. The preferred building blocks for isolating spacers are amino acids with rigid, extended conformations such as proline, isonipecotic acid, and tert-leucine. Replacing isolating spacers by conventional N- and C-caps dramatically increases the helicity of dodecaalanine. Solubilized, isolated polyalanines provide optimal tools for testing polypeptide helicity algorithms, central to resolution of the protein folding problem.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Short, solubilized polyalanines are conformational chameleons: exceptionally helical if N- and C-capped with helix stabilizers, weakly to moderately helical if capped with rigid spacers.
pubmed:affiliation
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
pubmed:publicationType
Journal Article, Comparative Study, 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