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It is necessary to conserve structural and functional integrity of the bone tissue during normal physiological conditions.
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In functionally diverse enzyme superfamilies (SFs), conserved structural and active site features reflect catalytic capabilities 'hard-wired' in each SF architecture.
It can be constructed using any reliable protein domain definition, where domains are defined as evolutionarily conserved structural and functional protein units.
Although distantly related to plant or animal RNAi machinery components, these diatom proteins possess conserved structural and functional domains including key amino acid residues that support their potential role in the small RNA pathways described above.
One of the challenges still facing researchers and field engineers in implementing and making down-hole tubular technology cost effective is to conserve structural integrity of tubular.
Previously, we have found that a step size of 0.1 Å and displacement along 2 modes was most appropriate in term of conserving structural quality and computational efficiency.
They have conserved structural features and catalytic domains yet show huge variation at different domains resulting in a variety of functions.
The identified conserved structural elements and amino acids are likely to be important for the function of the domain and will help to guide future studies of the LytR-CpsA-Psr proteins.
The putative amino acid sequence of the polyprotein precursor gene of RabV 97-103 has been translated; based on the amino acid alignment with WNV, the putative mature proteins, conserved structural elements, and putative enzyme motifs were localized.
The long-timescale MD simulations reported here support the notion of a simple and evolutionarily conserved structural mechanism controls homo- and heterodimerization of Her2, and thereby Her2 activation.
Unlike the highly conserved structural RNAs (rRNAs and tRNAs) or small microRNAs, the lincRNA genes closely resemble protein-coding genes in terms of diversity, size, and gene architecture.
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