PubMed · 5942243
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L G Wayne. 1966. Mycobacterial classification.. https://doi.org/10.1164/arrd.1966.93.6.958
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Interactions of Ins(1,2,6)P3 (IP), with spermine (Spm) and zinc cations have been studied by potentiometric and 31P NMR titrations. In the 4-11 pH range, two IPSpmZn2H3 and IPSpmZn2H mixed complexes are formed which are largely predominant with respect to the binary species. According to 31P NMR titration it is likely that one of the zinc cations preferably binds phosphates P1 and P6. The adduct formation between Ins(1,2,6)P3 and spermine seems also favourable to the formation of the mixed complexes. The occurrence of ternary complexes involving inositol-phosphates, biogenic amines, and metallic cations may be of relevance in the regulation of biological processes.
The effect of infrared low-intensity laser irradiation on functional activity of blood polymorphonuclear leukocytes was studied in vitro. A dose-dependent priming of polymorphonuclear leukocytes induced by infrared low-intensity laser irradiation was demonstrated. Similar effects were also observed in the presence of the photosensitizer photosense.
Experimental and simulation studies can complement each other nicely in the area of protein folding. Experiment reports on the average properties of a large ensemble (approx. 10(17)-10(19) molecules), typically over time. Molecular dynamics simulations, on the other hand, provide detailed information for a single molecule, a component of the ensemble. By combining these approaches we can obtain not only a more complete picture of folding, but we can also take advantage of the strengths of different methods. For example, experiment cannot provide molecular structures. Molecular dynamics simulations can provide such information, but the simulations are meaningless without a linked experiment. Thus, the interrelated nature of simulation in assessing experimental assumptions and in providing structures to augment energetic descriptions, and experiment in judging whether the simulations are reasonable, provides more confidence in the resulting information about folding. This combination yields tested and testable molecular models of states that evade characterization by conventional methods. Therefore, we have explored the combined use of these methods to map folding/unfolding pathways at atomic resolution, in collaboration with Alan Fersht. Here we focus on chymotrypsin inhibitor 2, a small single-domain, two-state folding protein.