Two-state models of protein folding kinetics | Zendy

Robert Zwanzig | Zendy

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Two-state models of protein folding kinetics

Author(s) -

Robert Zwanzig

Publication year - 1997

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.94.1.148

Subject(s) - protein folding , folding (dsp implementation) , downhill folding , kinetics , reaction rate constant , thermodynamics , chemistry , kinetic energy , folding funnel , phi value analysis , lattice protein , physics , biochemistry , classical mechanics , electrical engineering , engineering

The folding of some proteins appears to be a two-state kinetic process. A two-state kinetic model is justified if protein molecules rapidly equilibrate between different unfolded conformations prior to complete folding. Here I show that this rapid equilibration is a natural consequence of reasonable assumptions about reaction rate constants and folding thermodynamics.

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