Linked Life Data

8918936

Source:http://linkedlifedata.com/resource/pubmed/id/8918936

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-12-23
pubmed:abstractText
Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural information on isotopically labeled recombinant sperm whale apomyoglobin in the native state at pH 6.1. Assignments for backbone resonances (1HN, 15N, and 13Calpha) have been made for a large fraction of the residues in the protein. The secondary structure indicated by the observed chemical shifts is nearly identical to that found in carbonmonoxy-holomyoglobin in all assigned regions. In addition the chemical shifts themselves are highly similar in both proteins. This suggests that the majority of the apomyoglobin polypeptide chain adopts a well defined structure which is very similar to that of holomyoglobin. However, backbone resonances from a contiguous region of the apoprotein, corresponding to the EF loop, the F helix, the FG loop, and the beginning of the G helix, are broadened beyond detection due to conformational fluctuations. We propose that the polypeptide in this region exchanges between a holoprotein-like conformation and one or more unfolded or partially folded states. Such a model can explain the current NMR data, the charge state distributions observed by mass spectrometry, and the effects of mutagenesis. Apomyoglobin possesses many of the characteristics of a native, globular protein and does not adhere to the classical description of a molten globule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
531-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Is apomyoglobin a molten globule? Structural characterization by NMR.
pubmed:affiliation
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.