Secondary structure and rigidity in model proteins
โ Scribed by Perticaroli, Stefania; Nickels, Jonathan D.; Ehlers, Georg; O'Neill, Hugh; Zhang, Qui; Sokolov, Alexei P.
- Book ID
- 120992646
- Publisher
- Royal Society of Chemistry
- Year
- 2013
- Tongue
- English
- Weight
- 545 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1744-683X
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๐ SIMILAR VOLUMES
A thermodynamic model describing formation of alpha-helices by peptides and proteins in the absence of specific tertiary interactions has been developed. The model combines free energy terms defining alpha-helix stability in aqueous solution and terms describing immersion of every helix or fragment
Chemical shift data have been collected on eight proteins that have the same conformation in solution as in their crystal structures. Ring-current shifts have been calculated and subtracted from the experimentally measured shifts, to leave shifts that depend only on local conformation. Overall, the