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SITE-DIRECTED MUTAGENESIS OF GROEL:DEVELOPING A SYSTEM FOR MONITORING ALLOSTERIC MOVEMENTS BY FLUORESCENCE RESONANCE ENERGY TRANSFER
The Escherichia coli chaperonin protein GroEL can assist protein folding to its native state through the consumption of ATP. Accompanying this process, GroEL undergoes structural change, resulting in an expansion of the ...
One-Dimensional Free Energy Surface Models of Protein Folding: Connecting Theory and Experiments
Experimental techniques have now reached the sub-microsecond timescale necessary to study fast events in protein folding. However, analysis of fast folding experiments still commonly rely on conventional procedures that ...
Barrier Heights and Diffusion Coefficients in Protein Folding
A widely held view with respect to the folding of single-domain proteins is that they are two-state. In other words, it is seemingly sufficient to invoke just two thermodynamic macrostates - folded and unfolded - to explain ...
Molecular Interactions of Ubiquitin and Polyubiquitin with Ubiquitin Binding Domains
Ubiquitin is a small protein that is covalently attached to proteins, either as a single ubiquitin moiety or as polyubiquitin chains. A cascade of enzymatic reactions is required for the isopeptide linkage between the ...