Linked Life Data

20135035

Source:http://linkedlifedata.com/resource/pubmed/id/20135035

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-2-5
pubmed:abstractText
Alpha helices are useful scaffolds to build biologically active peptides. The intrinsic stability of an alpha-helix is a key feature that can be successfully designed, and it is governed by the constituting amino acid residues. Their individual contributions to helix stability are given, according to Lifson-Roig theory, by their w parameters, which are known for all proteinogenic amino acids, but not for non-natural ones. On the other hand, non-natural, conformationally-restricted amino acids can be used to impart biochemical stability to peptides intended for in vivo administration. Efficient design of peptides based on these amino acids requires the previous determination of their w parameters. We begin here this task by determining the w parameters of two restricted analogs of alanine: (alpha-methyl)alanine and 1-aminocyclopropanecarboxylic acid. According to their w values (alpha-methyl)alanine is almost as good a helix forming residue as alanine, while 1-aminocyclopropanecarboxylic acid is, similarly to proline, a helix breaker.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1477-0539
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
788-92
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine.
pubmed:affiliation
Department of Organic Chemistry, ICMA, Universidad de Zaragoza-CSIC, Pedro Cerbuna 12, 50009 Zaragoza, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't