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PMID: 3843533 Published · ppublish English Journal Article

Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin.

European biophysics journal : EBJ ·Vol. 13 ·No. 2 ·1985-00-00 ·Pages 109-21

Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bychkova VE, Gilmanshin RI, Lebedev YuO, Semisotnov GV, Tiktopulo EI, Ptitsyn OB

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.

MeSH Terms
Animals Cattle Circular Dichroism Female Kinetics Lactalbumin/isolation & purification Magnetic Resonance Spectroscopy Milk Protein Conformation Protein Denaturation Thermodynamics Viscosity X-Ray Diffraction
Chemicals
Lactalbumin
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Dolgikh D A
Abaturov L V
Bolotina I A
Brazhnikov E V
Bychkova V E
Gilmanshin R I
Lebedev YuO
Semisotnov G V
Tiktopulo E I
Ptitsyn O B
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Article Info
Journal
European biophysics journal : EBJ
Abbr.
Eur Biophys J
ISSN
0175-7571
DOI
10.1007/BF00256531
Published
1985-00-00
Pages
109-21
Language
English
Region
Germany
NLM ID
8409413
Subset
IM
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1007/BF00256531 View journal details
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