Literature summary for 2.7.4.3 extracted from

Whitford, P.C.; Gosavi, S.; Onuchic, J.N.
Conformational transitions in adenylate kinase. Allosteric communication reduces misligation (2008), J. Biol. Chem., 283, 2042-2048.

Search for more literature for 2.7.4.3

Application

Application	Comment	Organism
analysis	coarse grained model for the interplay between protein structure, folding and function which is applicable to allosteric or non-allosteric proteins. High strain energy is correlated with localized unfolding during the functional transition. Competing native interactions from the open and closed form can account for the large conformational transitions. Local unfolding may be due, in part, to competing intra-protein interactions	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
coarse grained model for the interplay between protein structure, folding and function. High strain energy is correlated with localized unfolding during the functional transition. Competing native interactions from the open and closed form can account for the large conformational transitions. Local unfolding may be due, in part, to competing intra-protein interactions	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69441	-	-

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Release 2023.1 (January 2023)