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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.
Direct NMR observation of a transient folding intermediate provides new evidence for the importance of molten globules as general intermediates in protein folding.
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.
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.
