A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in γS-crystallin

Keyphrases

• N-terminal Domain 100%
• Crystallin 100%
• Mutant Protein 100%
• Globular Domain 100%
• Destabilizing mutations 100%
• Unfolding Intermediates 66%
• Exchange Rate 66%
• Core Residue 66%
• Guanidinium Chloride 66%
• Cataract 33%
• Vertebrates 33%
• Conformational Change 33%
• Atomic Force Microscopy 33%
• Neurological Diseases 33%
• Age-related Illnesses 33%
• Amyloid Fibrils 33%
• Free Energy 33%
• Surface Loops 33%
• Room Temperature 33%
• Fibril Structure 33%
• Stress-related 33%
• Hydrogen-deuterium Exchange 33%
• Denaturants 33%
• Highly Stable 33%
• Native Protein 33%
• High Temperature 33%
• Elevated Temperature 33%
• Well Structure 33%
• Thioflavin T 33%
• Cellular Organization 33%
• Folded Proteins 33%
• Unfolded Proteins 33%
• Eye Lens 33%
• Partial Unfolding 33%
• Folding-unfolding 33%
• Near-native 33%
• Structured Surface 33%

Biochemistry, Genetics and Molecular Biology

• N-Terminus 100%
• Crystallin 100%
• Mutant Protein 75%
• C-Terminus 50%
• Guanidinium Chloride 50%
• Conformational Change 25%
• Atomic Force Microscopy 25%
• Hydrogen-Deuterium Exchange 25%
• Room Temperature 25%
• Thioflavin 25%
• Amyloid Protein 25%