Conformational Entropy of Intrinsically Disordered Proteins from Amino Acid Triads
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep11740.pdf
Reference58 articles.
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3. Karplus, M., Ichiye, T. & Pettitt, B. M. Configurational entropy of native proteins. Biophys. J. 52, 1083–1085 (1987).
4. Sapienza, P. J. & Lee, A. L. Using NMR to study fast dynamics in proteins: methods and applications. Curr. Opin. Pharmacol. 10, 723–730 (2010).
5. Thompson, J. B., Hansma, H. G., Hansma, P. K. & Plaxco, K. W. The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy. J. Mol. Biol. 322, 645–652 (2002).
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