Article
The length of a single turn controls the overall folding rate of "three-fingered" snake toxins.
Biochemistry - 17 Nov 1998
Ruoppolo M, Moutiez M, Mazzeo M F, Pucci P, Ménez A, Marino G, Quéméneur E
Abstract excerpt
Snake curaremimetic toxins are short all-beta proteins, containing several disulfide bonds which largely contribute to their stability. The four disulfides present in snake toxins make a "disulfide beta-cross"-fold that was suggested to be a good protein folding template. Previous studies on the...
Topics
- Alkylation
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Cobra Neurotoxin Proteins
- Erabutoxins
- Mass Spectrometry
- Molecular Sequence Data
- Mutation
- Peptide Mapping
- Protein Folding
- Protein Structure, Secondary