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Equilibrium folding–unfolding pathways of model proteins: Effect of myoglobin–heme contacts
Author(s) -
Jernigan Robert L.,
Miyazawa Sanzo
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220113
Subject(s) - chemistry , myoglobin , folding (dsp implementation) , protein folding , native state , contact order , heme , random coil , downhill folding , molten globule , equilibrium unfolding , crystallography , chemical physics , folding funnel , hemeprotein , biophysics , phi value analysis , circular dichroism , biochemistry , enzyme , electrical engineering , biology , engineering
The equilibrium of protein folding–unfolding has been investigated with a simple two‐state, native and random‐coil, model; we have termed this the globule–coil model. Energies are calculated by favoring native long‐range contact pairs. Most‐probable native domains are obtained at all stages of the transition; plausible folding pathways are constructed by connecting these domains by assuming simple growth. Even though native heme–protein contacts represent less than 6% of the total number of native contact pairs, their inclusion appears to change the folding pathway of apomyoglobin from the growth and merging of two native domains to the growth of a single domain. This indicates that pathways derived with this method may be critically sensitive to the details of the contact map and physical constraints during the folding process.