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Calorimetric study of the heat and cold denaturation of beta-lactoglobulin

Biochemistry

Sep 22, 1992

Y V Griko, Peter L Privalov

PMID: 1390668

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Abstract

Temperature-induced changes of the states of beta-lactoglobulin have been studied calorimetrically. In the presence of a high concentration of urea this protein shows not only heat but also cold denaturation. Its heat denaturation is approximated very closely by a two-state transition, ...read more

Mentioned in this Paper

Thermodynamics
Orthophosphate
Lactoglobulins
Circular Dichroism, Vibrational
Protein Conformation
Calorimetry
Common Cold
Carmol
Protein Denaturation
Cold Temperature
Paper Details
References
  • References16
  • Citations64
  • References16
  • Citations64
12345...

Calorimetric study of the heat and cold denaturation of beta-lactoglobulin

Biochemistry

Sep 22, 1992

Y V Griko, Peter L Privalov

PMID: 1390668

DOI:

Abstract

Temperature-induced changes of the states of beta-lactoglobulin have been studied calorimetrically. In the presence of a high concentration of urea this protein shows not only heat but also cold denaturation. Its heat denaturation is approximated very closely by a two-state transition, ...read more

Mentioned in this Paper

Thermodynamics
Orthophosphate
Lactoglobulins
Circular Dichroism, Vibrational
Protein Conformation
Paper Details
References
  • References16
  • Citations64
  • References16
  • Citations64
12345...

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