| Literature DB >> 3843533 |
D A Dolgikh, L V Abaturov, I A Bolotina, E V Brazhnikov, V E Bychkova, R I Gilmanshin, G V Semisotnov, E I Tiktopulo, O B Ptitsyn.
Abstract
We describe a novel physical state of a protein molecule which is nearly as compact as the native state and has pronounced secondary structure, but differs from the native state by the large increase of thermal fluctuations (in particular, by the large mobility of side groups). This state has been characterized in detail for the acid form of bovine alpha-lactalbumin as a result of the study of physical properties of this state by a large variety of different methods (hydrodynamics, diffuse X-ray scattering, circular dichroism and infrared spectra, polarization of the luminescence, proton magnetic resonance, deuterium exchange and microcalorimetry). It has been shown that bovine alpha-lactalbumin can be transformed into a similar state by thermal denaturation. This process is thermodynamically two state (i.e. all-or-none transition), which means that this state differs from the native one by a phase transition of the first order.Entities:
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Year: 1985 PMID： 3843533 DOI： 10.1007/bf00256531
Source DB: PubMed Journal: Eur Biophys J ISSN： 0175-7571 Impact factor: 1.733