Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2006-4-19
pubmed:abstractText
The elastic properties of capsids of the cowpea chlorotic mottle virus have been examined at pH 4.8 by nanoindentation measurements with an atomic force microscope. Studies have been carried out on WT capsids, both empty and containing the RNA genome, and on full capsids of a salt-stable mutant and empty capsids of the subE mutant. Full capsids resisted indentation more than empty capsids, but all of the capsids were highly elastic. There was an initial reversible linear regime that persisted up to indentations varying between 20% and 30% of the diameter and applied forces of 0.6-1.0 nN; it was followed by a steep drop in force that is associated with irreversible deformation. A single point mutation in the capsid protein increased the capsid stiffness. The experiments are compared with calculations by finite element analysis of the deformation of a homogeneous elastic thick shell. These calculations capture the features of the reversible indentation region and allow Young's moduli and relative strengths to be estimated for the empty capsids.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-10585969, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-11607035, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-12484982, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-12881484, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-13031234, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-14525215, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-15133147, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-15386271, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-15542144, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-15571723, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-15600887, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-16381893, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-2610349, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-4924992, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-7642706, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-7886952, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-8806492, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-9007078, http://linkedlifedata.com/resource/pubmed/commentcorrection/16606825-9581792
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6184-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't