Turtle hemoglobin: evidence of a T-state oxyhemoglobin |
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Authors: | S R Louro G Bemski |
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Affiliation: | Departamento de Física, Pontifícia Universidade Católica, Cx.P. 38071, Rio de Janeiro, RJ, Brasil |
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Abstract: | The 270 MHz 1H NMR spectra of rabbit skeletal long and short S2 were indistinguishable at 20°C and 30°C and contained only a small proportion of sharp peaks associated with flexible regions. At 60°C both proteins were denatured and had essentially identical spectra. At 40°C and 50°C the long S2 spectrum contained a marginally greater proportion of sharp peaks, representing not more than 25 residues/chain. Our results are consistent with the presence of a small hinge in long S2 but do not support its containing an extensive region which provides contractile force by a helix—coil transition. |
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Keywords: | Photosystem I Photosystem II P700 Rieske iron—sulfur center |
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