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The enhanced stability of a cold shock protein from a thermophilic organism, compared to its counterpart from a mesophile, results mainly from a single change in amino acid sequence that improves electrostatic interactions among the charged groups on the protein surface.
Neuronal-Sec1 and syntaxin 1a, two proteins essential for membrane fusion, have now been crystallized in a complex with each other. The structure shows how the horseshoe-shaped nSec1 surrounds and holds syntaxin in a new conformation, and suggests that conformational changes in both nSec1 and syntaxin must take place for membrane fusion to proceed.
Large ribozymes collapse to compact structures that are non-native and partially disordered when folding is induced by magnesium ions. This suggests that the early steps in the folding of these RNAs are non-specific.