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The biologically active carboxy-terminal peptide of the G-protein receptor, rhodopsin, forms a compact structure, suggesting that it is a structural domain in this integral membrane protein. The disposition of serines explains receptor kinase specificity.
Low-temperature laser experiments provide insight into the rough energy landscape of myoglobin, strengthen the evidence for a hierarchical organization of the protein, and allow tantalizing glimpses into the dynamics of proteins.
In cytochrome c, the unfolding reaction occurs in four discreet stops, as monitored by the exchange of solvent hydrogen for backbone aminde hydrogens under varying denaturant concentrations.