Linked Life Data

6300068

Source:http://linkedlifedata.com/resource/pubmed/id/6300068

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1983-5-5
pubmed:abstractText
DNA binding protein II from Bacillus stearothermophilus has been purified as a single species from the nonribosomal cell fraction by a combination of gel filtration and ion exchange chromatography. The protein occurs in solution as a tetramer and is able to bind to 30 S, 50 S, and 70 S ribosomal particles. Circular dichroism studies show that the protein has approximately 45% alpha-helix. The secondary structure of the Bacillus protein is considerably more resistant to the effects of increasing temperature and urea concentration than the homologous protein (NS1 and NS2) from Escherichia coli. Proton magnetic resonance experiments show that the protein has a well folded, compact tertiary structure. The DNA binding protein has been crystallized from several precipitants as monoclinic needles and triclinic plates. The monoclinic form diffracts to at least 3.5 A and oscillation data from the native crystals have been collected. The protein is able to bind to both single- and double-stranded oligodeoxyribonucleotides. Upon binding, several changes occur in the protein NMR spectrum which may be used for further analysis of the mechanism of interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4003-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
On the DNA binding protein II from Bacillus stearothermophilus. I. Purification, studies in solution, and crystallization.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't