Linked Life Data

18307988

Source:http://linkedlifedata.com/resource/pubmed/id/18307988

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2008-3-10
pubmed:abstractText
It is generally accepted that in the c-type cytochromes the covalently bound heme plays a primary role in the acquisition of the folded state. Here, we show that a stabilized site-directed variant of apo-cyt c551 from Pseudomonas aeruginosa (Pa-apocyt F7A/W77F) retains native-like features in the presence of sodium sulfate even in the absence of heme. By time-resolved intrinsic fluorescence, we have evidence that Pa-apocyt F7A/W77F may acquire a compact, native-like conformation within microseconds. These results challenge current thinking about the role of the heme group in the folding of c-type cytochromes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
582
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1003-7
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Fast folding kinetics and stabilization of apo-cytochrome c.
pubmed:affiliation
Dipartimento di Scienze Biochimiche, A. Rossi Fanelli, Sapienza, Università di Roma, Piazzale A. Moro 5, 00185 Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't