Calorimetry of proteins and nucleic acids.
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.
Plum
G E
GE
Department of Chemistry, Rutgers, State University of New Jersey, Piscataway 08855, USA.
Breslauer
K J
KJ
D002151:Calorimetry; D002152:Calorimetry, Differential Scanning; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D017186:Titrimetry
D011506:Proteins; D012313:RNA; D004247:DNA