Findings from this study highlight the importance of field-informed appraisals of landscape dynamics, site-specific characteristics and the imprint of historical (evolutionary) context in making such comparative assessments.
Here, we elucidate detailed events of substrate binding, through a combination of crystallography, molecular dynamics, site-directed mutagenesis, biochemical/biophysical assays, and the design and synthesis of novel ligands.
Here, we elucidate the structural basis of ligand binding to Mhp1 and the consequent movements of individual amino acids and overall conformational changes using a combination of X-ray crystallography, molecular dynamics, site-directed mutagenesis, ligand design, synthetic chemistry and biochemical/biophysical assays.
For example, at 25 °C, the dynamics of site 3 are invariant, within error, upon addition of salts or glycine.
Detailed analysis of the data collected at 10 °C, however, reveals that dynamics at site 3 are reduced upon addition of MgCl2 and glycine.
An additional result supporting the lack of relevance of the local treatment on the metastatic process is provided by the analysis of DM dynamics by site that yields results substantially identical to what was obtained for patients undergoing mastectomy [ 4].
These abandonments exhibit contrasting environmental dynamics: smaller sites are observed to preferentially re-establish saltmarsh; larger sites more commonly revert to unvegetated tidal flat.
We studied the dynamics of site-specific recombination by the resolvase encoded by the Escherichia coli transposon Tn3.
To study the navigational dynamics of sites of this type, it is necessary to look at the combination of all navigational aids.
