Counting the calories to stay in the groove.
High-sensitivity microcalorimetry is beginning to make an impact on the determination of thermodynamic parameters associated with protein-DNA interactions and the understanding of the relationship of these data to structural details of complex formation.
Ladbury
J E
JE
Oxford Centre for Molecular Sciences, University of Oxford, New Chemistry Laboratory, UK.
D001426:Bacterial Proteins; D001483:Base Sequence; D001665:Binding Sites; D002151:Calorimetry / Q000379:methods*; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008832:Microchemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics; D029968:Escherichia coli Proteins
D001426:Bacterial Proteins; D004247:DNA; D011506:Proteins; D012097:Repressor Proteins; C027190:TRPR protein, E coli; D029968:Escherichia coli Proteins