A Calorimetric Study of the Denaturation of Lysozyme by Guanidine Hydrochloride and Hydrochloric Acid
- 1 October 1971
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 22 (3) , 345-349
- https://doi.org/10.1111/j.1432-1033.1971.tb01550.x
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozymeJournal of the American Chemical Society, 1971
- Thermodynamics of proton ionization in dilute aqueous solution. XIII. .DELTA.G.deg.(pK), .DELTA.H.deg., and .DELTA.S.deg. values for proton ionization from several methyl- and ethyl-substituted aliphatic carboxylic acids at 10, 25, and 40.deg.Journal of the American Chemical Society, 1970
- Thermodynamics of the denaturation of ribonuclease by guanidine hydrochlorideBiochemistry, 1970
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. III. Dependence on temperatureBiochemistry, 1970
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25°Biochemistry, 1969
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25°Biochemistry, 1969
- A Flow Micro Reaction Calorimeter.Acta Chemica Scandinavica, 1968
- Design and Testing of a Micro Reaction Calorimeter.Acta Chemica Scandinavica, 1968
- Proteins as random coils. IV. Osmotic pressures, second virial coefficients, and unperturbed dimensions in 6M guanidine hydrochlorideJournal of the American Chemical Society, 1967
- Proteins as random coils. III. Optical rotatory dispersion in 6M guanidine hydrochlorideJournal of the American Chemical Society, 1967