Linked Life Data

7008840

Source:http://linkedlifedata.com/resource/pubmed/id/7008840

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-5-13
pubmed:abstractText
The aromatic residues of fd coat protein in sodium dodecyl sulfate micelles are characterized by 1H and 13C NMR. Resonances from both types of nuclei show structure-induced chemical shift dispersion and line widths indicative of a folded native structure for the protein. The two tyrosines were found to have pKas of 12.3 and 12.5 by 1H NMR and spectrophotometric titrations. 13C relaxation measurements show that two of the three Phe rings have significant internal mobility, the two Tyr rings have moderate internal mobility, and the Trp side chain is completely immobilized. Qualitative comparisons are made between the intact virus and the isolated coat protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
290-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Hydrogen-1 and carbon-13 nuclear magnetic resonance of the aromatic residues of fd coat protein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't