Linked Life Data

10101837

Source:http://linkedlifedata.com/resource/pubmed/id/10101837

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-4-14
pubmed:abstractText
The reversible, oriented immobilization of proteins on solid surfaces is a prerequisite for the investigation of molecular interactions and the controlled formation of supramolecular assemblies. This paper describes a generally applicable method using a synthetic chelator thioalkane that can be self-assembled on gold surfaces. The reversible binding of an anti-lysozyme F(ab) fragment modified with a C-terminal hexahistidine extension was monitored and the apparent dissociation constants determined using surface plasmon resonance. Infra-red spectroscopy demonstrated that the secondary structure of the protein was unaffected by the immobilization process. The retention of functionality of the immobilized protein was also successfully demonstrated. Given the mild reaction conditions and reversibility, this method of oriented immobilization of proteins opens possibilities for the development of biosensors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0956-5663
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-61
pubmed:dateRevised
2009-7-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Immobilization of histidine-tagged proteins on gold surfaces using chelator thioalkanes.
pubmed:affiliation
Laboratoire de chimie physique des polymères et membranes, Ecole Polytechnique Fédérale de Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't