Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1982-7-19
pubmed:abstractText
The sites of energy transduction within the human hemoglobin molecule for the regulation of oxygen affinity have been determined by an extensive study of the molecule's energetic response to structural alteration at individual amino acid residues. For 22 mutant and chemically modified hemoglobins we have determined the total free energy used by the tetrameric molecule for alteration of oxygen affinity at the four binding steps. The results imply that the regulation of oxygen binding affinity is due to energy changes which are mostly localized at the alpha 1 beta 2 interface. They also indicate a high degree of "internal cooperativity" within this contact region--i.e., the structural perturbations at individual residue sites are energetically coupled. Cooperativity in ligand binding is thus a reflection of cooperativity at a deeper level--that of the protein-protein interactions within the alpha 1 beta 2 interfacial domain.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-1152051, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-1152063, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-1276133, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-16058681, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-18205, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-22548, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-234399, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-235541, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-265575, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-27380, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-284341, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-35218, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-382987, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-39173, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-40974, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4200894, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-423967, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4361855, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4426396, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4436316, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4436327, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4530985, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-460437, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-469939, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4725657, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4728965, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4765360, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-4808644, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-481225, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-500721, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-5368335, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-5422014, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-5528785, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-640853, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-6787056, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-6790544, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-694508, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7016880, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7074009, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7204092, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7238856, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7248452, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7326236, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7329280, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7430145, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-7451499, http://linkedlifedata.com/resource/pubmed/commentcorrection/6952235-999811
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1849-53
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.
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