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avena/cárie dentária

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A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain.

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Phototropins are autophosphorylating serine/threonine kinases responsible for blue-light perception in plants; their action gives rise to phototropism, chloroplast relocation, and opening of stomatal guard cells. The kinase domain constitutes the C-terminal part of Avena sativa phototropin 1. The
The kinetics of the microsecond phototransformation intermediates of 124 kDa Avena phytochrome (I700(1,2) were studied in the presence of bound monoclonal antibodies at various temperatures. A global analysis was applied to the decays at all wavelengths at each temperature in order to derive the
Oat (Avena sativa L.) seedling extract exhibited a high degree of catalytic activities. Bioinformatics were used to identify β-amylases as abundant enzymes in the oat seedling extract. These identified oat enzymes are a member of the GH14 family. Proteins in the Avena sativa seedling extract were

In silico analysis of DREB transcription factor genes and proteins in grasses.

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Plants are exposed to various environmental stresses, including drought, salinity, low temperature, etc. Dehydration responsive element binding (DREB) genes, the members of AP2/ERF transcription factor family, regulate the biological processes against cold and dehydration stresses. In this study, we

Primary photochemistry of the dark- and light-adapted states of the YtvA protein from Bacillus subtilis.

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The primary (100 fs to 10 ns) and secondary (10 ns to 100 μs) photodynamics in the type II light-oxygen-voltage (LOV) domain from the blue light YtvA photoreceptor extracted from Bacillus subtilis were explored with transient absorption spectroscopy. The photodynamics of full-length YtvA were

Identification of a new oat β-amylase by functional proteomics.

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Oat (Avena sativa L.) seed extracts exhibited a high degree of catalytic activity including amylase activities. Proteins in the oat seed extracts were optimized for their amylolytic activities. Oat extract with amylolytic activity was separated by SDS-PAGE and a major protein band with an apparent
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