Linked Life Data

2558737

Source:http://linkedlifedata.com/resource/pubmed/id/2558737

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-3-1
pubmed:abstractText
A method for distinguishing between membrane and soluble proteins in an amino acid sequence was developed, using only two parameters associated with the hydrophobicity: the average hydrophobicity and the power spectral density of period longer than 30 residues. The power spectral density was calculated by a maximum entropy method of Fourier transformation. Membrane proteins could be distinguished from soluble proteins with a distinction rate as high as 97%. This fact strongly suggests that the morphology of proteins, i.e., membrane or soluble forms, is determined thermodynamically through the hydrophobicity of polypeptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-77
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
A theoretical method for distinguishing between soluble and membrane proteins.
pubmed:affiliation
Department of Material Systems Engineering, Faculty of Technology, Tokyo University of Agriculture and Technology, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't