Disulfide bond plasticity in epidermal growth factor
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference18 articles.
1. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints
2. Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-αtransforming growth factors
3. Human type-.alpha. transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements
4. The Disulfide Folding Pathway of Human Epidermal Growth Factor
5. Reexamination of the Folding of BPTI: Predominance of Native Intermediates
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3. Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern;Nature Communications;2019-10-28
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