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Single-domain proteins folding kinetics

Most small, single-domain proteins display thermodynamic and kinetic signatures of two-state folders. The simplicity of this folding scenario, in which only unfolded (U) and native (N) states are populated to any significant degree, led to the development of kinetic models analogous to those first introduced in the context of chemical rate processes. [Pg.202]


See other pages where Single-domain proteins folding kinetics is mentioned: [Pg.28]    [Pg.29]    [Pg.30]    [Pg.41]    [Pg.397]    [Pg.182]    [Pg.176]    [Pg.38]    [Pg.115]    [Pg.429]    [Pg.17]    [Pg.181]    [Pg.12]    [Pg.124]    [Pg.729]    [Pg.149]    [Pg.155]    [Pg.155]    [Pg.145]    [Pg.62]    [Pg.29]    [Pg.67]   
See also in sourсe #XX -- [ Pg.36 , Pg.37 ]




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Domain single

Domains folding

Domains protein

Fold domain

Folding kinetics

Kinetic folding

Kinetics protein folding

Kinetics proteins

Single-domain proteins

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