Linked Life Data

12833258

Source:http://linkedlifedata.com/resource/pubmed/id/12833258

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-6-30
pubmed:abstractText
The solution structure of the central repetitive domain of high molecular weight (HMW) wheat gluten proteins has been investigated for a range of concentrations and temperatures using mainly small-angle neutron scattering. A representative part of the repetitive domain (dB1) was studied as well as an "oligomer" basically consisting of four dB1 units, which has a length similar to the complete central domain. The scattering data over the entire angular range of both proteins are in quantitative agreement with a structural model based on a worm-like chain, a model frequently used in polymer theory. This model describes the "supersecondary structure" of dB1 and dB4 as a semiflexible cylinder with a length of about 235 and 900 A, respectively, and a cross-sectional diameter of about 15 A. The flexibility of both proteins is characterized by a persistence length of about 13 A. Their structures are thus quantitatively identical, which implies that the central HMW domain can be elongated while retaining its structural characteristics. It seems conceivable that the flexible cylinder results from a helical structure, which resembles the beta-spiral observed in earlier studies on gluten proteins and elastin. However, compared to the previously proposed structure of a (stiff) rod, our experiments clearly indicate flexibility of the cylinder.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2003 Wiley Periodicals, Inc. Biopolymers 69: 311-324, 2003
pubmed:issnType
Print
pubmed:volume
69
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
311-24
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. I. Small-angle neutron scattering.
pubmed:affiliation
University of Edinburgh, Department of Physics and Astronomy, James Clerk Maxwell Building, Mayfield Road, Edinburgh EH9 3JZ, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't