To avoid crystallographic artifacts, the search for protein-protein interaction interfaces was conducted only on those pairs of protein chains of the Asymmetric Unit that were present with the same relative orientation in at least one of the Biological Units assigned by the authors of the structure.
Before this study, a formative evaluation of the DiAs user interface was conducted to evaluate the feasibility of the design for patient use.
An elucidation of the structures of the NBD that interacted directly with the coupling helices during the targeted MD simulation at this transmission interface was conducted, and the results are listed in Table 1.
Microstructure analysis and measurements of interface intermetallic growth were conducted using samples after 0, 1000, 2000 and 3000 thermal cycles.
With the knowledge that FAD binds tightly and cooperatively to AidB, along with crystal structures showing FAD engaged in numerous interactions at the AB dimer interface, AUC experiments were conducted to determine if AidB is monomeric in the absence of flavin.
To understand the interface properties, several tests were conducted to examine the various characteristics of specimens with different layer interfaces.
Microscopy studies on coupled interface and bearing plane were conducted to understand the damage mechanism.
Structured searches were conducted in MEDLINE (PubMed interface), EMBASE (OVID interface), Cochrane Central (OVID interface) and grey from their start date onwards.
Two usability studies with 23 subjects and two eye-tracking studies with 21 subjects were conducted with this interface and paper, PDF, and spreadsheet interfaces.
In the encapsulation phase, the workflow and function of the bioinformatics software were conducted, the encapsulation interfaces were designed, and the runtime interaction between users and computers was simulated.
