Pages that link to "Q42162394"

The following pages link to Folding thermodynamics and kinetics of the leucine-rich repeat domain of the virulence factor Internalin B (Q42162394):

Displaying 16 items.

• Crystal structure of an engineered YopM-InlB hybrid protein (Q27682510) (← links)
• Disorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretion (Q28083580) (← links)
• Structural, thermodynamic, and phosphatidylinositol 3-phosphate binding properties of Phafin2. (Q30274857) (← links)
• Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models (Q30375581) (← links)
• Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment (Q33888074) (← links)
• Complex energy landscape of a giant repeat protein (Q34635963) (← links)
• Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability (Q35590129) (← links)
• Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins (Q37394818) (← links)
• Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein (Q38871119) (← links)
• The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway (Q39132517) (← links)
• C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein (Q41438086) (← links)
• Diffuse transition state structure for the unfolding of a leucine-rich repeat protein. (Q41524471) (← links)
• Characterization of the unfolded state of repeat proteins (Q41829482) (← links)
• What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding? (Q41899145) (← links)
• The Variable Regions of Lactobacillus rhamnosus Genomes Reveal the Dynamic Evolution of Metabolic and Host-Adaptation Repertoires (Q41950562) (← links)
• A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP. (Q46274343) (← links)