Linked Life Data

6758862

Source:http://linkedlifedata.com/resource/pubmed/id/6758862

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-3-11
pubmed:abstractText
The frequency dependence of the proton spin lattice relaxation time of bovine serum albumin, muscle tissue, Micrococcus luteus and yeast has been measured by the aid of the field-cycling technique. In all systems 14N1H-quadrupole dips have been observed. The conclusion is that amide groups are the dominating relaxation centers up to approx. 10(7) Hz. This finding can be understood by the fact that protein backbone fluctuations and, if possible, tumbling of the whole molecule rather than side group motions are the relevant mechanisms in this frequency range. A proton relaxation scheme for cells and tissue is presented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
719
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
292-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
NMR field-cycling relaxation spectroscopy of bovine serum albumin, muscle tissue, Micrococcus luteus and yeast. 14N1H-quadrupole dips.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't