Legume lectins constitute a family of proteins in which small alterations arising from sequence variations in essentially the same tertiary structure lead to large changes in quaternary association. All of them are dimers or tetramers made up of dimers. Dimerization involves side-by-side or back-to-
Is re-association in folded proteins a case of nonextensivity?
โ Scribed by Constantino Tsallis; George Bemski; Renio S Mendes
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 149 KB
- Volume
- 257
- Category
- Article
- ISSN
- 0375-9601
No coin nor oath required. For personal study only.
โฆ Synopsis
Pioneering experiments by Frauenfelder and collaborators have shown that the ligands of iron CO, O in heme proteins 2 ) ลฝ
) such as myoglobin and hemoglobin, when photo-dissociated at temperatures up to about T for example, T s 160 K for . ลฝ . MbCO in glycerol-water exhibit an anomalous power-law, instead of exponential rebinding behavior as a function of time. We show here that this behavior is consistent with nonextensive statistics that have been successfully applied to other physical phenomena.
๐ SIMILAR VOLUMES
In a study of 70 cases of trisomy 18 and 450 matched controls in the second trimester we have measured the maternal serum levels of the analytes alpha feto protein (AFP), free -human chorionic gonadotrophin (hCG) and pregnancy associated plasma protein-A (PAPP-A). We have found the median multiple o