P
Peter L. Privalov
Researcher at Johns Hopkins University
Publications - 150
Citations - 20639
Peter L. Privalov is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Denaturation (biochemistry) & Globular protein. The author has an hindex of 66, co-authored 149 publications receiving 20030 citations. Previous affiliations of Peter L. Privalov include University of Alberta & Russian Academy of Sciences.
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Book ChapterDOI
Stability of Proteins Small Globular Proteins
TL;DR: 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.
Journal ArticleDOI
A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
TL;DR: The thermal properties of five globular proteins with known spatial structure, ribonuclease, lysozyme, chymotrypsin, cytochrome c and myoglobin, are investigated by scanning microcalorimetry and it is shown that heat-denaturation of these proteins can be described to a first approximation by the two-state transition model.
Book ChapterDOI
Stability of protein structure and hydrophobic interaction.
TL;DR: This chapter focuses on the stability of protein structure and hydrophobic interaction, and examines the main achievements of microcalorimetric studies of protein denaturation and of the dissolution of nonpolar substances in water.
Book ChapterDOI
Stability of proteins. Proteins which do not present a single cooperative system
TL;DR: The practical importance of thermodynamic studies of protein stability—that is, its importance not only for understanding the principles of organization of these molecules, but just for obtaining structural information on the domain level is emphasized.
Book ChapterDOI
Energetics of protein structure.
TL;DR: This chapter summarizes the experimental information on protein energetics and investigates the correlation between thermodynamic and structural characteristics of protein, including the water-ASA of various groups in the native and unfolded states, the number of hydrogen bonds, and the extent of van der Waals contacts in thenative state.