Linked Life Data

21609877

Source:http://linkedlifedata.com/resource/pubmed/id/21609877

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-5-25
pubmed:abstractText
Protein folding has been studied extensively in vitro, but much less is known about how folding proceeds in vivo. A particular distinction of folding in vivo is that folding begins while the nascent polypeptide chain is still undergoing synthesis by the ribosome. Studies of cotranslational protein folding are inherently much more complex than classical in vitro protein folding studies, and historically there have been few methods available to produce the quantities of pure material required for biophysical studies of the nascent chain, or assays to specifically interrogate its conformation. However, the past few years have produced dramatic methodological advances, which now place cotranslational folding studies within reach of more biochemists, enabling a detailed comparison of the earliest stages of protein folding on the ribosome to the wealth of information available for the refolding of full-length polypeptide chains in vitro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1557-7988
pubmed:author
pubmed:copyrightInfo
Copyright © 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
466
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-90
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Measuring cotranslational folding of nascent polypeptide chains on ribosomes.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
pubmed:publicationType
Journal Article