PubMed · 12025626
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S King. 1998. Multistate licensure analysis.. https://pubmed.ncbi.nlm.nih.gov/12025626/
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A new integrated sequence-structure database, called IADE (Integrated ASTRAL-DSSP-EMBL), incorporating matching mRNA sequence, amino acid sequence, and protein secondary structural data, is constructed. It includes 648 protein domains. Based on the IADE database, we studied the relation between RNA stem-loop frequencies and protein secondary structure. It was found that the alpha-helices and beta-strands on proteins tend to be preferably "coded" by mRNA stem region, while the coils on proteins tend to be preferably "coded" by mRNA loop region. These tendencies are more obvious if we observe the structural words (SWs). An SW is defined by a four-amino-acid-fragment that shows the pronounced secondary structural (alpha-helix or beta-strand) propensity. It is demonstrated that the deduced correlation between protein and mRNA structure can hardly be explained as the stochastic fluctuation effect.
The deuterium spin-lattice relaxation times in (D2) ligands of W, Ru and Os complexes are reviewed and analyzed in terms of the fast internal (D2) motions: free rotation, librations and 180 degrees jumps. The analysis was performed using quadrupolar coupling constant (DQCC) parameters taken from the solid-state 2H NMR spectra and density function theory calculations. It is shown that the calculated DQCC values can be corrected for further use in interpretations of deuterium relaxation times for Ru and Os dihydrogen complexes. The resulting data led to a criterion for using the relaxation data to distinguish fast-spinning dihydrogen ligands. It is shown that the principal components of electric field gradient tensors at D in the dihydrogen ligands are oriented closer to M-D directions.
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