Linked Life Data

20857395

Source:http://linkedlifedata.com/resource/pubmed/id/20857395

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-11-24
pubmed:abstractText
The 57-amino acid human salivary polypeptide P-B has been synthesized by the solid-phase method using 9-fluorenylmethoxycarbonyl (Fmoc) strategy. The circular dichroism (CD) spectroscopy, Fourier-transform infrared spectroscopy (FTIR) and molecular modeling methods have been used for conformational studies of P-B. Examination of the CD spectra of P-B showed the content of the secondary structure to be independent of temperature over the range 0-60 °C at pH = 7 as well as over the pH range of 2-12 at 37 °C. P-B adopts predominantly unordered structure with locally appearing ?-turns. The cumulative results obtained using the CD and FTIR spectroscopic techniques indicate the percentage of the polyproline type-II (PPII) helix being as low as about 10%. Similarly, the molecular dynamics (MD) simulations reveal only a short PPII helix in the C-terminal fragment of the peptide (Pro(51)-Pro(54)), which constitutes 7%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1099-1387
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
709-15
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Synthesis and conformational analysis of salivary proline-rich peptide P-B.
pubmed:affiliation
University of Gda?sk, Sobieskiego 18, Gda?sk, Poland. kamysz@chem.univ.gda.pl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't