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Structural bioinformatics using a recently developed backbone nomenclature assisted in the rapid evaluation of the backbone behavior.
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Initially, most of the scores used in structure prediction assessment aimed at the evaluation of the protein backbone or fold, thereby focusing on carbon α (Cα) atom positions.
The iterative and closely linked process involving the design (and redesign) of MIC-O-MAP and its evaluation formed the backbone of our research process.
Evaluation of RNA backbone conformations is difficult for both computational and experimental approaches.
This two-state classification allows precise evaluation of the effect of base flipping on local backbone degrees of freedom.
However, evaluation of the root-mean-square deviation (rmsd) of the protein backbone atoms (C, CA, and N) among variants and WT hBChE showed marked differences.
Ulmer, T. S., Ramirez, B. E., Delaglio, F. & Bax, A. Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy.
Cut down either side of the backbone and discard the backbone.
Evaluation of the young team.
Evaluation of the VarCall model.
Evaluation of the geological evidence.
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