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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1991-10-4
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pubmed:abstractText |
The shielding of lysine groups from acetylation by acetic anhydride has been used to identify the regions of calmodulin in contact with melittin in the 1:1 complex. The estimation of the degree of acetylation was done by examining cyanogen bromide and cyanogen bromide/trypsin digests by mass spectrometry. Evidence was obtained that lysines-21, -75, and -148 are protected to some extent, with the implication that both the N- and C-terminal lobes and the connecting strand are involved in the interaction.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0003-2697
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
196
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
120-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1888025-Acetylation,
pubmed-meshheading:1888025-Amino Acid Sequence,
pubmed-meshheading:1888025-Animals,
pubmed-meshheading:1888025-Calmodulin,
pubmed-meshheading:1888025-Cattle,
pubmed-meshheading:1888025-Cyanogen Bromide,
pubmed-meshheading:1888025-Male,
pubmed-meshheading:1888025-Mass Spectrometry,
pubmed-meshheading:1888025-Melitten,
pubmed-meshheading:1888025-Molecular Sequence Data,
pubmed-meshheading:1888025-Peptide Mapping,
pubmed-meshheading:1888025-Spectrometry, Mass, Fast Atom Bombardment,
pubmed-meshheading:1888025-Thrombin,
pubmed-meshheading:1888025-Triticum,
pubmed-meshheading:1888025-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Maryland (Baltimore County) 21228.
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pubmed:publicationType |
Journal Article
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