Equilibrium folding–unfolding pathways of model proteins: Effect of myoglobin–heme contacts

✍ Scribed by Robert L. Jernigan; Sanzo Miyazawa

• Publisher: Wiley (John Wiley & Sons)
• Year: 1983
• Tongue: English
• Weight: 444 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360220113

✦ Synopsis

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 a t 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 he critically sensitive to the details of the contact map and physical constraints during the folding process.