Linked Life Data

19169452

Source:http://linkedlifedata.com/resource/pubmed/id/19169452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-1-26
pubmed:abstractText
This tutorial review outlines the modern ligation methods that enable the efficient total chemical synthesis of enzymes and other protein molecules. Key to this success is the chemoselective reaction of unprotected synthetic peptides ('chemical ligation'). Notably, native chemical ligation enables the reaction of two unprotected peptides in aqueous solution at neutral pH to form a single product in near quantitative yield. Full-length synthetic polypeptides are folded to form the defined tertiary structure of the target protein molecule, which is characterized by mass spectrometry, NMR, and X-ray crystallography, in addition to biochemical and/or biological activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0306-0012
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
338-51
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Total chemical synthesis of proteins.
pubmed:affiliation
Department of Chemistry, Institute for Biophysical Dynamics, Center for Integrative Science, University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA. skent@uchicago.edu
pubmed:publicationType
Journal Article, Review