Stability of proteins: small globular proteins.
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Summary
The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system, and the temperature-induced changes in protein, denaturational and predenaturational changes inprotein, thermodynamics of protein unfolding, and thermodynamic properties of protein.
- Type
- review
- Published
- 1979-01-01
- Cited by
- 1,963
- References
- 157
- OpenAlex
- https://openalex.org/W1496368635
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:39993450
Keywords
Globular protein, Denaturation (fissile materials), Potentiometric titration, Native state, Chemistry
References
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- Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride.
- Evidence for residual structure in acid- and heat-denatured proteins.
- Calorimetric determination of denaturation enthalpy for lysozyme in guanidine hydrochloride.
- Structural studies and organic ligand-binding properties of bovine plasma albumin.
- An experimental approach to the study of the folding of staphylococcal nuclease.
Cited by
- Partial molar volumes of the amino acid side‐chains of proteins in aqueous solution: Some comments on their estimation using partial molar volumes of amino acids and small peptides
- Protein-protein interaction: an analysis by computer simulation.
- Characterization of a reversible denaturational transition occurring in the case of an irreversibly denaturing membrane spanning protein.
- Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution
- Heat and cold denaturation of phosphoglycerate kinase (interaction of domains)
- Thermodynamic parameters for protein-protein and protein-ligand interaction by differential scanning microcalorimetry.
- Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom.
- Differential scanning calorimetry of proteins.
- Enthalpy and heat capacity changes for the reduction of insulin.
- Domains in the fibrinogen molecule.
- Gibbs free energy of adsorption for biomolecules in ion-exchange systems.
- Structural and thermodynamic aspects of the hydrophobic effect.
- Structural energetics of the molten globule state
- Ligand-binding interactions and stability.
- Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance
- Consistency in structural energetics of protein folding and peptide recognition
- Emerging themes in RNA folding.
- Folding rate dependence on the chain length of RNA-like heteropolymers.
- What should the Z‐score of native protein structures be?
- Heat capacity of hydrogen-bonded networks: an alternative view of protein folding thermodynamics.
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