Residual Dipolar Couplings for Resolving Cysteine Bridges in Disulfide-Rich Peptides

Disulfide bridges in proteins are formed by the oxidation of pairs of cysteine residues. These cross-links play a critical role in stabilizing the 3D-structure of small disulfide rich polypeptides such as hormones and venom toxins. The arrangement of the multiple disulfide bonds directs the peptide...

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Detalles Bibliográficos
Autores principales: Ramanujam, Venkatraman, Shen, Yang, Ying, Jinfa, Mobli, Mehdi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6987419/
https://www.ncbi.nlm.nih.gov/pubmed/32039137
http://dx.doi.org/10.3389/fchem.2019.00889

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6987419/
https://www.ncbi.nlm.nih.gov/pubmed/32039137
http://dx.doi.org/10.3389/fchem.2019.00889

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