SpringerProtocols: Abstract: Microcalorimetry of Proteins and Their Complexes

1. Microcalorimetry of Proteins and Their Complexes

By: Peter L. Privalov²

Abstract

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Ultrasensitive microcalorimetric techniques for measuring the heat capacities of proteins in dilute solutions over a broad temperature range (DSC) and the heats of protein reactions at fixed temperatures (ITC) are described and the methods of working with these instruments are considered. Particular attention is paid to analyzing the thermal properties of individual proteins, their stability, the energetics of their folding, and their association with specific macromolecular partners. Use of these calorimetric methods is illustrated with examples of small compact globular proteins, small proteins having loose noncompact structure, multidomain proteins, and protein complexes, particularly with DNA.

Affiliation(s): (2) Department of Biology, Johns Hopkins University, Baltimore, MD, USA

Book Title: Protein Structure, Stability, and Interactions

Series: Methods in Molecular Biology | Volume: 490 | Pub. Date: Mar-01-2008 | Page Range: 1-39 | DOI: 10.1007/978-1-59745-367-7_1

Subject: Protein Science

Key Words: microcalorimetry - proteins - complexes - folding - stability - energetics

References

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