• Publications
  • Influence
Stability of proteins: small globular proteins.
  • P. Privalov
  • Chemistry, Medicine
  • Advances in protein chemistry
  • 1979
Publisher Summary The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system. Protein is aExpand
  • 1,858
  • 46
Energetics of protein structure.
Publisher Summary This chapter summarizes the experimental information on protein energetics. This field is developing fast and the concept of the energetics of protein structure has changedExpand
  • 878
  • 26
Scanning microcalorimetry in studying temperature-induced changes in proteins.
  • 677
  • 20
Cold denaturation of proteins.
  • P. Privalov
  • Chemistry, Medicine
  • Critical reviews in biochemistry and molecular…
  • 1990
This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea andExpand
  • 229
  • 17
A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.
The thermal properties of five globular proteins with known spatial structure, ribonuclease, lysozyme, chymotrypsin, cytochrome c and myoglobin, are investigated by scanning microcalorimetry. It isExpand
  • 1,162
  • 14
Stability of protein structure and hydrophobic interaction.
Publisher Summary This chapter focuses on the stability of protein structure and hydrophobic interaction. The interest in hydrophobic interactions was stimulated by their unusual thermodynamicExpand
  • 1,091
  • 14
Stability of proteins. Proteins which do not present a single cooperative system.
  • P. Privalov
  • Chemistry, Medicine
  • Advances in protein chemistry
  • 1982
Publisher Summary The chapter discusses the protein stability with emphasis on compact globular proteins representing a single cooperative system. All the small compact globular proteins representExpand
  • 986
  • 11
Common features of protein unfolding and dissolution of hydrophobic compounds.
Protein unfolding and the dissolution of hydrophobic compounds (including solids, liquids, and gases) in water are characterized by a linear relation between entropy change and heat capacity change.Expand
  • 360
  • 11
Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect.
The partial molar heat capacities of various peptides and various organic compounds that model the amino acid side-chains or their parts in aqueous solution have been determined by precise scanningExpand
  • 404
  • 10
Interpreting protein/DNA interactions: distinguishing specific from non-specific and electrostatic from non-electrostatic components
We discuss the effectiveness of existing methods for understanding the forces driving the formation of specific protein–DNA complexes. Theoretical approaches using the Poisson–Boltzmann (PB) equationExpand
  • 138
  • 10
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