PubMed · 1518798
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J Aqvist. 1992. Comments on models for electrostatic effects in proteins.. https://doi.org/10.1093/protein%2F5.5.469
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The effect of salt and temperature on the interaction of homo-oligonucleotides with a derivatized Sepharose CL-6B hydrophobic support has been explained by the application of two different models: the solvophobic theory and the preferential interaction analysis. It has been shown that the two approaches give adequate descriptions of the experimental results. The models were used in order to estimate, respectively the parameter C, which is proportional to the reduction in hydrophobic exposed surface area upon adsorption, and the number of water and salt ions released upon adsorption. It was concluded that the magnitude of these parameters can be strongly influenced by the temperature, the hydrophobicity of the bases of the nucleotides, the molecular mass of the oligonucleotides and the presence of secondary structures. Parameter C was quantitatively related with the number of water molecules and salt ions released upon adsorption. These parameters were found to correlate linearly in cases where structural changes with temperature are not significant.
Recently, residual dipolar couplings (RDCs) of backbone N-HN vectors measured in 11 different alignment media were analyzed with respect to structure and dynamics in a model-free way in terms of generalized order parameters and motional anisotropies. The anisotropies in the central alpha-helix were found to be strikingly uniformly distributed. In this communication, these parameters are further interpreted in terms of physically feasible cooperative reorientational motion of the helix with respect to the core of the protein. The RDCs are compatible with a model in which all N-HN vectors of the alpha-helix of ubiquitin exhibit correlated anisotropic excursions with amplitudes of 21 degrees and 12 degrees along two orthogonal directions x' ' and y' ' of a coordinate system C' ', if z' ' represents the helix axis. Such motion contradicts neither NOE data nor molecular force-field calculations.