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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-1-27
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pubmed:abstractText |
The relationship between different amino acids at the beta 6 position of hemoglobin and tetramer stability was addressed by a site-directed mutagenesis approach. Precipitation rates during mechanical agitation of oxyhemoglobins with Gln, Ala, Val, Leu and Trp at the beta 6 position increased 2, 5, 13, 21 and 53 times, respectively, compared with that for Hb A. There was a linear relationship between the log of the precipitation rate constant and amino acid hydrophobicity at the beta 6 position, suggesting that enhanced precipitation of oxy Hb S during mechanical agitation results in part from increased hydrophobicity of beta 6 Val. Deoxyhemoglobin solubility increased in the order of beta 6 Ile, Leu, Val, Trp, Gln, Ala and Glu suggesting that hydrophobic interactions between beta 6 Val and the acceptor site of another hemoglobin molecule during deoxy-Hb S polymerization not only depend on hydrophobicity but also on stereospecificity of the amino acid side chain at the beta 6 position. Furthermore, our results indicate that hydrophobic amino acids at the beta 6 position which promote tetramer instability in the oxy form do not necessarily promote polymerization in the deoxy form.
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pubmed:grant | |
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 |
Jan
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
315
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8416810-Hemoglobins,
pubmed-meshheading:8416810-Humans,
pubmed-meshheading:8416810-Mutagenesis, Site-Directed,
pubmed-meshheading:8416810-Oxyhemoglobins,
pubmed-meshheading:8416810-Protein Conformation,
pubmed-meshheading:8416810-Protein Denaturation,
pubmed-meshheading:8416810-Recombinant Proteins,
pubmed-meshheading:8416810-Solubility,
pubmed-meshheading:8416810-Stress, Mechanical,
pubmed-meshheading:8416810-Structure-Activity Relationship
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pubmed:year |
1993
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pubmed:articleTitle |
Effects of beta 6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramers.
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pubmed:affiliation |
Children's Hospital of Philadelphia, Department of Pediatrics, PA 19104.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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