Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference31 articles.
1. Structural Characterization of a Partly Folded Apomyoglobin Intermediate
2. Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study
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5. Structural Characterization of the Molten Globule and Native States of Apomyoglobin by Solution X-ray Scattering
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Misfolding and Amyloid Aggregation of Apomyoglobin;International Journal of Molecular Sciences;2013-07-09
2. W-F Substitutions in Apomyoglobin Increase the Local Flexibility of the N-terminal Region Causing Amyloid Aggregation: A H/D Exchange Study;Protein & Peptide Letters;2013-06-01
3. Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F;European Biophysics Journal;2012-06-22
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