Linked Life Data

2911722

Source:http://linkedlifedata.com/resource/pubmed/id/2911722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4887
pubmed:dateCreated
1989-2-22
pubmed:abstractText
The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
85-8
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structural origins of high-affinity biotin binding to streptavidin.
pubmed:affiliation
Central Research & Development Department, E. I. du Pont de Neumours and Company, Inc., Wilmington, DE 19880-0228.
pubmed:publicationType
Journal Article