Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance. [electronic resource]
Producer: 19820120Description: 4955-9 p. digitalISSN:- 0027-8424
- Anion Exchange Protein 1, Erythrocyte
- Blood Proteins -- metabolism
- Electron Spin Resonance Spectroscopy
- Erythrocyte Membrane -- metabolism
- Erythrocytes -- metabolism
- Glyceraldehyde-3-Phosphate Dehydrogenases -- metabolism
- Humans
- Membrane Proteins -- metabolism
- Motion
- Protein Conformation
- Solubility
- Spin Labels
- Viscosity
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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