Linked Life Data

10742185

Source:http://linkedlifedata.com/resource/pubmed/id/10742185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-5-12
pubmed:abstractText
Studies of classic zinc-finger peptides over the past 15 years have offered insights into the coupled processes of metal binding and protein folding. Within the past two years, this insight has been used to increase our understanding of the importance of first and second shell contributions (i.e. contributions from direct and indirect metal ligands) to metal binding and protein-folding stability, and led to advances in de novo protein design and protein redesign.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
162-5
pubmed:dateRevised
2009-8-25
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Zinc-dependent protein folding.
pubmed:affiliation
Center for Environmental Bioinorganic Chemistry, Department of Geosciences, Princeton University, Princeton, 08544, USA. ehcox@princeton.edu
pubmed:publicationType
Journal Article, Review