Linked Life Data

2245405

Source:http://linkedlifedata.com/resource/pubmed/id/2245405

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-1-10
pubmed:abstractText
Human polymorphic epithelial mucins (PEM) are high molecular weight glycoproteins that are associated with breast cancer. Recent structural studies have identified that the protein core of PEM contains a 20 amino acid tandem repeat that has elements of secondary structure which coincide with the epitopes for a number of tumour reactive antibodies. In our continuing structural studies we have now investigated the use of the scanning tunneling microscope (STM) to directly image the conformation of the twenty amino acid PEM core peptide. High resolution STM images reveal that the peptide has an overall topography similar to that predicted by molecular modelling. The images identify directly that the free peptide is conformationally non-restricted and can adopt a number of discrete conformations in the solid state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0304-3835
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Scanning tunneling microscopy imaging of the tumour associated antigenic 20 amino acid human polymorphic epithelial mucin core peptide fragment.
pubmed:affiliation
VG STM Laboratory for Biological Applications, Department of Pharmaceutical Sciences, University of Nottingham, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't