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Heat capacity changes upon burial of polar and nonpolar groups in proteins
Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C ' position of the C-capping box of alpha-helices
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability