Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and ‘molten globule’ states
- 1 August 1986
- journal article
- research article
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 8 (4) , 231-236
- https://doi.org/10.1016/0141-8130(86)90032-2
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- α-Lactalbumin: A calcium metalloproteinPublished by Elsevier ,2004
- ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chainsFEBS Letters, 1983
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- Detection and characterization of the intermediate on the folding pathway of human .alpha.-lactalbuminBiochemistry, 1978
- A folding model of α-lactalbumin deduced from the three-state denaturation mechanismJournal of Molecular Biology, 1977
- Study of thermal denaturation of lysozyme and other globular proteins by light‐scattering spectroscopyBiopolymers, 1976
- Three-state denaturation of α-lactalbumin by guanidine hydrochlorideJournal of Molecular Biology, 1976
- Change in the Ultraviolet Absorption of an Adenosine Triphosphate Analog, β-Naphthyl Triphosphate, during Its Hydrolysis by Heavy Meromyosin1The Journal of Biochemistry, 1975
- Study of the chemical denaturation of lysozyme by optical mixing spectroscopyBiochemistry, 1973
- Inter- and Intramolecular Interactions of α-Lactalbumin. II. Aggregation Reactions at Acid pH*Biochemistry, 1964