Molecular dynamics study of unfolding of lysozyme in water and its mixtures with dimethyl sulfoxide is observed between the results obtained using several different criteria. The
secondary structure according
Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis be distinguished from other
proteins in terms of lack of any fixed
structure. Such dynamic behavior of IDPs earned
Beta-rich intermediates in denaturation of lysozyme: accelerated molecular dynamics simulations of globular
proteins into fibrils is associated with global conformational rearrangement and involves
Evidence of oligomerization of bovine insulin in solution given by NMR. The presence of certain
secondary structure elements was revealed on a qualitative level based on nuclear
Protein intrinsic disorder toolbox for comparative analysis of viral proteins,
structure, and function. Location of each
protein within a virion, if known, is also denoted. Our analysis
Secondary structure and colloidal stability of beta-casein in microheterogeneous water-ethanol solutions-association and the
secondary structure in a wide range of temperatures and ethanol concentrations. Temperature induced
Calculation of chemical shift dispersion for α-CH protons in binase observed for α-CH protons of residues involved in
secondary structure could be explained assuming