Linked Life Data

18304786

Source:http://linkedlifedata.com/resource/pubmed/id/18304786

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-5-5
pubmed:abstractText
Adsorption of HIV protease onto surfaces that are usually considered to be protein-resistant was studied quantitatively using surface plasmon resonance. Adsorption onto gold surfaces functionalized by OH-terminated alkyl chains was much stronger than onto oligo(ethylene glycol)-terminated surfaces. Equilibrium and kinetic adsorption constants were determined. An anomalous mutual attraction between adsorbate molecules was observed, indicating the possibility of two-dimensional crystallization of HIV protease. These results are applicable for the design of sensors/biosensors for HIV protease resistance detection and for proper manipulation of this enzyme in laboratory devices.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0927-7765
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-9
pubmed:dateRevised
2009-10-16
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Anomalous adsorptive properties of HIV protease: indication of two-dimensional crystallization?
pubmed:affiliation
Institute of Chemical Technology, Department of Analytical Chemistry, Technická 5, 166 28 Prague 6, Czech Republic.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't