Calorimetry of proteins and nucleic acids

G. Eric Plum; Kenneth J. Breslauer

doi:10.1016/0959-440X(95)80062-X

Calorimetry of proteins and nucleic acids

G. Eric Plum, Kenneth J. Breslauer

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

Abstract

The availability of sensitive calorimetric instrumentation has led to a considerable increase in thermodynamic studies of proteins, nucleic acids, and their interactions. This article reviews some of the recent contributions of calorimetry to characterizing the thermodynamic origins of protein and nucleic acid stability and conformational preferences, as well as the interactions of proteins with each other, with small molecules, and with nucleic acids.

Original language	English (US)
Pages (from-to)	682-690
Number of pages	9
Journal	Current Opinion in Structural Biology
Volume	5
Issue number	5
DOIs	https://doi.org/10.1016/0959-440X(95)80062-X
State	Published - Oct 1995

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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10.1016/0959-440X(95)80062-X

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title = "Calorimetry of proteins and nucleic acids",

abstract = "The availability of sensitive calorimetric instrumentation has led to a considerable increase in thermodynamic studies of proteins, nucleic acids, and their interactions. This article reviews some of the recent contributions of calorimetry to characterizing the thermodynamic origins of protein and nucleic acid stability and conformational preferences, as well as the interactions of proteins with each other, with small molecules, and with nucleic acids.",

author = "Plum, {G. Eric} and Breslauer, {Kenneth J.}",

year = "1995",

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AU - Breslauer, Kenneth J.

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N2 - The availability of sensitive calorimetric instrumentation has led to a considerable increase in thermodynamic studies of proteins, nucleic acids, and their interactions. This article reviews some of the recent contributions of calorimetry to characterizing the thermodynamic origins of protein and nucleic acid stability and conformational preferences, as well as the interactions of proteins with each other, with small molecules, and with nucleic acids.

AB - The availability of sensitive calorimetric instrumentation has led to a considerable increase in thermodynamic studies of proteins, nucleic acids, and their interactions. This article reviews some of the recent contributions of calorimetry to characterizing the thermodynamic origins of protein and nucleic acid stability and conformational preferences, as well as the interactions of proteins with each other, with small molecules, and with nucleic acids.

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U2 - 10.1016/0959-440X(95)80062-X

DO - 10.1016/0959-440X(95)80062-X

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AN - SCOPUS:0028825912

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Calorimetry of proteins and nucleic acids

Abstract

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