Published August 1, 1972
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Journal Article
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Conformational studies of various hemoglobins by natural-abundance 13C NMR spectroscopy
- Creators
- Moon, R. B.
- Richards, J. H.
Abstract
Studies of variously liganded hemoglobins (both from human and rabbit) by natural-abundance 13C NMR spectroscopy have revealed apparent conformational differences that have been interpreted on the basis of two quaternary structures for the α2ß2 tetramer, and variable tertiary structures for the individual α and ß subunits. In solution, rabbit hemoglobins appear to have somewhat more flexibility than human hemoglobins.
Additional Information
© 1972 by the National Academy of Sciences. Communicated by Harry B. Gray, May 25, 1972. Contribution no. 4409 from the Gates and Crellin Laboratories of Chemistry, California Institute of Technology, Pasadena, Calif. 91109.Files
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Additional details
- Eprint ID
- 7274
- Resolver ID
- CaltechAUTHORS:MOOpnas72
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2007-01-25Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field