A look back at the molten globule state of proteins: thermodynamic aspects
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/s12551-019-00527-0.pdf
Reference114 articles.
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3. Arai M, Kondrashkina E, Kayatekin C et al (2007) Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an α/β-type protein. J Mol Biol 368:219–229. https://doi.org/10.1016/j.jmb.2007.01.085
4. Bai JH, Xu D, Wang HR et al (1999) Evidence for the existence of an unfolding intermediate state for aminoacylase during denaturation in guanidine solutions. Biochim Biophys Acta 1430:39–45. https://doi.org/10.1016/S0167-4838(98)00282-9
5. Balbach J, Forge V, van Nuland NA et al (1995) Following protein folding in real time using NMR spectroscopy. Nat Struct Biol 2:865–870. https://doi.org/10.1038/nsb1095-865
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