Linked Life Data

2340261

Source:http://linkedlifedata.com/resource/pubmed/id/2340261

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1990-6-26
pubmed:abstractText
We have used X-ray absorption fine structure spectroscopy (XAFS) to study and compare the structure of concanavalin A in crystals and in aqueous solution. Significant differences were found between crystal and solution in the configuration of the transition-metal site of the protein. The metal has six ligands in solution but only five in the crystal. The ligand bond lengths are shorter in the crystal than in solution. The vibrational disorder in the crystal and possibly the corresponding bond length show a negative temperature dependence whereas in solution they vary normally with temperature. The anomalous temperature dependence in the crystal suggests that as the temperature decreases the protein molecules are subject to additional stresses, which are transmitted as a tensile stress at the metal site leading to distorted geometry and lengthening and weakening of metal-ligand bonds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3599-603
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Evidence from X-ray absorption fine structure spectroscopy for significant differences in the structure of concanavalin A in solution and in the crystal.
pubmed:affiliation
Department of Physics, University of Washington, Seattle 98195.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.