Which relies on procedures that use the protein structure deposited in databases usually uses a geometrical resolution

Which might lead to language bias and the omission of inconclusive or negative studies in non-English articles. Fourthly, neither Egger’s linear regression test nor Begg’s rank correlation test played a perfect role in the present meta-analysis owing to an insufficient number of studies. Finally, the studies included in the subgroup analysis were too few to improve the accuracy of results. In summary, our study showed that hypertension would increase cataract risk, and this association was independent of pathoglycemia, obesity and dyslipidemia. The results of subgroup analysis suggested a significant association between hypertension and PSC. These findings indicated that hypertension control would help to reduce cataract prevalence and related cataract surgery costs. To confirm these findings, further efforts should be made to make a better understanding of the potential biological mechanisms. Large-scale and long-term Nilotinib molecular weight randomized controlled trials in various populations should be carried out in future studies to provide more powerful evidence. The shape of, and the physico-chemical properties on the protein molecular surfaces govern the specific molecular interactions in protein-ligand complexes. Therefore, studies as diverse as those on protein folding, protein conformational stability, inter- and intra- protein interactions, molecular recognition and docking ; as well as applications-orientated ones, such as drug design, protein and peptide solubility, crystal packing, and enzyme catalysis, benefit from an accurate and precise representation of the molecular surfaces. Furthermore, for large, intricate protein complexes, such as ion-channels, mechano-sensitive channels, or molecular chaperones, where the biomolecular functionality occurs on the inner molecular surface of the complex, makes the precision of the representation of molecular surfaces even more imperative. A relatively under-studied aspect of the construction of molecular surfaces is the resolution at which the hydrophobicity is represented. Because the biomolecular recognition is a geometrically-localized and charge- and hydrophobicity-specific event, its accurate description requires the representation of molecular surfaces with the finest resolution possible. However, while the charges are atom-localized and therefore their representation at high spatial resolution is immediate, the assignment of hydrophobicity based on residues inherently translates into its representation at a much lower resolution than that for electrical properties. Several studies developed “atomic hydrophobicities” proposing different sets of atom types, but a sensitivity analysis regarding the number of atom types, as well as study comparing the protein molecular surfaces obtained using atom- or amino acid-level hydrophobicity is lacking. Separate from the physical resolution of hydrophobicity, i.e., at atom- or amino acid-level, the impact of using different geometrical resolutions for the construction of the molecular surface has been also relatively under-studied. Indeed, the representation of the molecular surface.

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