Linked Life Data

8307163

Source:http://linkedlifedata.com/resource/pubmed/id/8307163

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-11
pubmed:abstractText
Pertussis toxin, both complete and the B-oligomer, were imaged by atomic force microscopy (AFM), using specimens prepared by simple surface adsorption on mica without further manipulation. The spatial arrangement of the subunits of the B-oligomer was clearly resolved, representing the first protein quaternary structure obtained by AFM in situ. The results suggest that the B-oligomer is a flat pentamer with the two large subunits located next to each other, and the catalytic A-subunit situated at the center above. We found that the B-pentamer was structurally stable for temperatures up to 60 degrees C and within the pH range of 4.5-9.5. It is also demonstrated that the AFM was capable of resolving features down to 0.5 nm on the B-oligomers, indicating its great potential for structural determination.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
338
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-92
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Structure and stability of pertussis toxin studied by in situ atomic force microscopy.
pubmed:affiliation
Department of Molecular Physiology & Biological Physics, University of Virginia, Charlottesville 22908.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't