Biophysical studies of protein solubility and amorphous aggregation by systematic mutational analysis and a helical polymerization model
Author:
Funder
Japan Society for the Promotion of Science
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology,Biophysics
Link
http://link.springer.com/article/10.1007/s12551-017-0342-y/fulltext.html
Reference32 articles.
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2. Arisaka F, Noda H, Maruyama K (1975) Kinetic analysis of the polymerization process of actin. Biochim Biophys Acta 400(2):263–274
3. Baldwin RL (2012) Gas–liquid transfer data used to analyze hydrophobic hydration and find the nature of the Kauzmann–Tanford hydrophobic factor. Proc Natl Acad Sci U S A 109(19):7310–7313
4. Boatz JC, Whitley MJ, Li M, Gronenborn AM, van der Wel PCA (2017) Cataract-associated P23T gammaD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Nat Commun 8:15137
5. Hall D, Minton AP (2002) Effects of inert volume-excluding macromolecules on protein fiber formation. I. Equilibrium models. Biophys Chem 98(1–2):93–104
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