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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6470
|
pubmed:dateCreated |
1994-4-19
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pubmed:abstractText |
A water-soluble, 62-residue, di-alpha-helical peptide has been synthesized which accommodates two bis-histidyl haem groups. The peptide assembles into a four-helix dimer with 2-fold symmetry and four parallel haems that closely resemble native haems in their spectral and electrochemical properties, including haem-haem redox interaction. This protein is an essential intermediate in the synthesis of molecular 'maquettes', a novel class of simplified versions of the metalloproteins involved in redox catalysis and in energy conversion in respiratory and photosynthetic electron transfer.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
368
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
425-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8133888-Amino Acid Sequence,
pubmed-meshheading:8133888-Drug Design,
pubmed-meshheading:8133888-Electrochemistry,
pubmed-meshheading:8133888-Electron Transport Complex III,
pubmed-meshheading:8133888-Hemeproteins,
pubmed-meshheading:8133888-Models, Molecular,
pubmed-meshheading:8133888-Molecular Sequence Data,
pubmed-meshheading:8133888-Oxidation-Reduction,
pubmed-meshheading:8133888-Protein Conformation,
pubmed-meshheading:8133888-Protein Structure, Secondary,
pubmed-meshheading:8133888-Spectrum Analysis
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pubmed:year |
1994
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pubmed:articleTitle |
Design and synthesis of multi-haem proteins.
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pubmed:affiliation |
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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