Linked Life Data

7546573

Source:http://linkedlifedata.com/resource/pubmed/id/7546573

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-10-27
pubmed:abstractText
One of the fundamental problems in macromolecular crystallography is the availability of the suitable heavy-atom derivatives necessary to solve the phase problem. The ability to label a protein with a tellurium-containing amino acid (telluromethionine) at internal sites through the utilization of protein biosynthesis supplies x-ray crystallographers a convenient phasing vehicle and nuclear magnetic resonance (NMR) spectroscopists an internal probe with which to study structure/function relationships via Te-125 NMR spectroscopy. In this communication we demonstrate the partial incorporation of telluromethionine into E. coli dihydrofolate reductase (DHFR) with no apparent perturbations to activity or substrate binding. Enzyme containing two moles TeMet exhibited a specific activity of 42 units/mg and a 1:1 binding ratio with methotrexate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1052-6781
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-34
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Telluromethionine in structural biochemistry.
pubmed:affiliation
Department of Chemistry, Tennessee Technological University, Cookeville 38505, USA.
pubmed:publicationType
Journal Article