Folding of ω-Conotoxins. 2. Influence of Precursor Sequences and Protein Disulfide Isomerase
Author:
Affiliation:
1. Department of Biology, University of Utah, Salt Lake City, Utah 84112
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9615755
Reference72 articles.
1. Solution structure of ω-conotoxin MVIIA using 2D NMR spectroscopy
2. The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima) Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from p
3. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
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