Linked Life Data

15882923

Source:http://linkedlifedata.com/resource/pubmed/id/15882923

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-7-15
pubmed:abstractText
Distribution of soft and rigid substructures within a protein molecule has been implicated in several occasions and most recently from the imaging and indentation experiments using an atomic force microscope. In this paper, previously reported result of mechanical extension experiments on the recombinant bovine carbonic anhydrase II, Q253C, is re-analyzed to estimate the distribution of Young's modulus, Y, in this protein. The force vs. extension curve of the enzymatically active, type I conformer gave an estimate of Y increasing from 40 to 220 MPa as the polypeptide chain was extended from 10 to 75 nm indicating the presence of a rigid core structure. The enzymatically inactive type II, in contrast, gave an almost constant modulus of 55+/-15 MPa in the same extension range in agreement with the previous proposal that it lacked a core structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Local rigidity of a protein molecule.
pubmed:affiliation
Laboratory of Biodynamics, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta Midoriku, Yokohama 226-8501, Japan. aikai@bio.titech.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't