Residual helical structure in the C-terminal fragment of cytochrome c
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00056a004
Reference32 articles.
1. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
2. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.
3. Helix-coil transition of the isolated amino terminus of ribonuclease
4. High-resolution three-dimensional structure of horse heart cytochrome c
5. Stabilization of helical structure in two 17-residue amphipathic analogues of the C-terminal peptide of cytochrome c
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