Tryptophan fluorescence provides a direct probe of nucleotide binding in the noncatalytic sites of Escherichia coli F₁-ATPase

Medicine & Life Sciences

• Adenine 18%
• Adenosine Diphosphate 61%
• Adenosine Monophosphate 17%
• Adenosine Triphosphate 60%
• benzo-ATP 74%
• Binding Sites 23%
• Catalysis 18%
• Catalytic Domain 27%
• Escherichia coli 54%
• Fluorescence 63%
• Fluorescence Resonance Energy Transfer 20%
• Guanosine Triphosphate 16%
• Hydrolysis 14%
• Inosine Diphosphate 25%
• Inosine Triphosphate 22%
• linear-benzoadenosine diphosphate 36%
• Magnesium 15%
• Nucleotides 62%
• Proton-Translocating ATPases 100%
• Site-Directed Mutagenesis 16%
• Tryptophan 82%

Chemistry

• Adenine 17%
• ADP 80%
• Binding Site 13%
• Catalysis 12%
• Donor 13%
• Drug Binding Parameter 23%
• Environment 10%
• Fluorescence 44%
• Fluorescence Resonance Energy Transfer 19%
• GDP 24%
• Hydrolysis 11%
• ITP 28%
• Nucleotide 63%
• Polarity 15%
• Probe 47%
• Site-Directed Mutagenesis 20%
• Tryptophan 71%