Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes

Keyphrases

• Fluorescence Studies 100%
• Intrinsic Fluorescence 100%
• Chaperonin GroEL 100%
• Ligand-induced Conformational Changes 100%
• Urea 66%
• GroEL 66%
• GroES 66%
• High Concentration 33%
• Tyrosine 33%
• Energy Transfer 33%
• Beta-gamma 33%
• Nucleotide Binding 33%
• Conformational Change 33%
• Adenosine 33%
• Molecular Mechanism 33%
• Chaperonin 33%
• Tryptophan 33%
• Tryptophan Fluorescence 33%
• Hydrophobic Probe 33%
• Transfer Test 33%
• Rhodanese 33%
• Co-chaperonin 33%
• Apical Domain 33%
• Bis-1 33%
• Imino 33%
• Triphosphate 33%
• In Vitro Refolding 33%
• Naphthalene Sulfonates 33%
• AMP-PNP 33%
• Tetradecamer 33%

Biochemistry, Genetics and Molecular Biology

• Conformational Change 100%
• Chaperonin 100%
• GroEL 100%
• Wild Type 66%
• Tryptophan 66%
• GroES 66%
• Tyrosine 33%
• Adenosine Triphosphate 33%
• Adenosine Diphosphate 33%
• Adenosine 33%
• Energy Transfer 33%
• Adenosine Monophosphate 33%
• Rhodanese 33%