Identification of surface residues in the trp repressor of Escherichia coli.
A subset of the spin systems assigned in the 1H NMR spectrum of the trp repressor in the first paper in this series (our penultimate preceding paper in this journal) can be identified as surface or buried residues on the basis of four independent types of measurement: selective spin-lattice relaxation times; the dependence of line widths on temperature and the concentration of manganous ion; fluorescence quenching; and titration behaviour. Criteria are developed for distinguishing surface and buried residues. The significance for the function of DNA binding proteins is discussed.
D001426:Bacterial Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese; D008433:Mathematics; D011487:Protein Conformation; D011522:Protons; D012097:Repressor Proteins / Q000032:analysis*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014157:Transcription Factors / Q000032:analysis*; D029968:Escherichia coli Proteins
D001426:Bacterial Proteins; D008345:Manganese; D011522:Protons; D012097:Repressor Proteins; D014157:Transcription Factors; C027190:TRPR protein, E coli; D029968:Escherichia coli Proteins