Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer

Keyphrases

• Distance Distribution 100%
• Time-resolved Fluorescence 100%
• Site-directed Spin Labeling 100%
• Phosphoglycerate Kinase 100%
• 3-phosphoglycerate 100%
• Domain Motion 100%
• Single-molecule Fluorescence Resonance Energy Transfer (smFRET) 100%
• Two-component Domains 100%
• Contact Area 50%
• Conformational Change 50%
• Conformational States 50%
• Interconversion 50%
• Fluorescence Lifetime 50%
• Catalytic Mechanism 50%
• Small Changes 50%
• Fluorescent Probe 50%
• Time-resolved 50%
• Transfer Techniques 50%
• Nonradiative Energy Transfer 50%
• Inner Surface 50%
• Site-directed mutagenesis 50%
• Genetic Engineering 50%
• Substrate Binding Site 50%
• Equilibrium Distribution 50%
• Average Distance 50%
• Mean Distance 50%
• Full Width at Half Maximum 50%
• Sub-nanosecond 50%
• Globular Domain 50%
• Conformational Substates 50%
• 3-phosphoglycerate Kinase 50%
• Engineered Cysteine 50%
• Phosphoryl Transfer 50%
• Hinge Bending 50%
• Nanosecond Time Scale 50%

Biochemistry, Genetics and Molecular Biology

• Motion 100%
• Fluorescence Energy Transfer 100%
• Phosphoglycerate Kinase 100%
• Solution and Solubility 66%
• Adenosine Triphosphate 66%
• Surface Property 33%
• Crystal Structure 33%
• Conformational Change 33%
• Catalytic Mechanism 33%
• Cysteine 33%
• Fluorescent Probe 33%
• Enzyme 33%
• Dynamics 33%
• Energy Transfer 33%
• Binding Site 33%
• Site-Directed Mutagenesis 33%