Linked Life Data

319831

Source:http://linkedlifedata.com/resource/pubmed/id/319831

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1977-4-28
pubmed:abstractText
The infrared spectrum of a structural lipoprotein from the Escherichia coli outer membrane indicated the lipoprotein had an alpha-helical conformation but no sign for the existence of beta-structures. From circular dichroism spectra of the lipoprotein, the alpha-helical content of the protein was found to be as high as 88% in 0.01-0.03% sodium dodecyl sulfate in the presence of 10(-5) M Mg2+ at pH 7.1 and 23 degrees C. When sodium dodecyl sulfate concentration increased higher than 0.1%, the alpha-helical content of the lipoprotein decreased to about 57%. Divalent cations, such as Mg2+ and Mn2+, were found to increase the helical content of the lipoprotein. The high alpha-helical content of the lipoprotein was observed in a wide range of temperatures (23 to 55 degrees C). The significance of the high alpha-helical content of the lipoprotein is discussed in light of the three-dimensional molecular models of the lipoprotein proposed previously.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
465
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
650-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Optical properties of an outer membrane lipoprotein from Escherichia coli.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.