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- Author:
- Dar, Tanveer A., et al. ; Danielson, Travis A.; Stine, Jessica M.; Briknarova, Klara; Bowler, Bruce E.; Show all 5 Authors
- Source:
- Biochemistry 2017 v.56 no.51 pp. 6662-6676
- ISSN:
- 1520-4995
- Subject:
- carbon; cytochrome c; guanidines; models; mutation; nitrogen; nuclear magnetic resonance spectroscopy; pH; protein secondary structure; stable isotopes; yeasts
- Abstract:
- ... There is considerable evidence that long-range interactions stabilize residual protein structure under denaturing conditions. However, evaluation of the effect of a specific contact on structure in the denatured state has been difficult. Iso-1-cytochrome c variants with a Lys54 → His mutation form a particularly stable His–heme loop in the denatured state, suggestive of loop-induced residual struc ...
- DOI:
- 10.1021/acs.biochem.7b01002
- PubMed:
- 29148740
- PubMed Central:
- PMC5751441
-
http://dx.doi.org/10.1021/acs.biochem.7b01002