Source:http://linkedlifedata.com/resource/pubmed/id/12403634
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
44
|
| pubmed:dateCreated |
2002-10-29
|
| pubmed:abstractText |
A circular permutein of sperm whale myoglobin in which the G helix is C-terminal, the H helix is N-terminal, and 16 amino acids link the H helix to the A helix has been expressed in Escherichia coli. The permutein sequence begins with Gly121 (using the numbering scheme for the wild-type protein) and terminates with Pro120. The ligand binding function of the permutein was assayed using stopped-flow methods and shown to be essentially identical to that of the wild-type protein. In addition, one- and two-dimensional NMR studies of the cyanomet isoform of the permutein show a nativelike structure with a heme binding pocket very similar to that of the wild-type myoglobin. Although the structure and function of the permutein resemble those of the wild-type myoglobin, the permutein is less stable to chemical denaturation by 5.2 kcal/mol.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
41
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
13318-27
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12403634-Amino Acid Sequence,
pubmed-meshheading:12403634-Animals,
pubmed-meshheading:12403634-Circular Dichroism,
pubmed-meshheading:12403634-Escherichia coli,
pubmed-meshheading:12403634-Ligands,
pubmed-meshheading:12403634-Molecular Sequence Data,
pubmed-meshheading:12403634-Myoglobin,
pubmed-meshheading:12403634-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12403634-Protein Binding,
pubmed-meshheading:12403634-Protein Denaturation,
pubmed-meshheading:12403634-Protein Engineering,
pubmed-meshheading:12403634-Protein Folding,
pubmed-meshheading:12403634-Protein Structure, Secondary,
pubmed-meshheading:12403634-Protein Structure, Tertiary,
pubmed-meshheading:12403634-Recombinant Proteins,
pubmed-meshheading:12403634-Thermodynamics,
pubmed-meshheading:12403634-Urea,
pubmed-meshheading:12403634-Whales
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
A circularly permuted myoglobin possesses a folded structure and ligand binding similar to those of the wild-type protein but with a reduced thermodynamic stability.
|
| pubmed:affiliation |
Department of Chemistry, Western Washington University, Bellingham, Washington 98225-9150, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|