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l threonine/çürük

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Theoretical calculations and surface morphology studies of L-threonine formate.

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In order to investigate microscopic second order nonlinear optical properties of L-threonine formate (abbreviated as LTF) crystals, the molecular dipole moment (μ), polarizability (α), and first hyperpolarizability (β) were computed using a series of basis sets including polarized and diffuse
The crystal structure of a L-threonine dehydrogenase (L-ThrDH; EC 1.1.1.103) from the psychrophilic bacterium Flavobacterium frigidimaris KUC-1, which shows no sequence similarity to conventional L-ThrDHs, was determined in the presence of NAD and a substrate analog, glycerol. The asymmetric unit
l-Threonine aldolases (l-TAs) catalyze the aldol condensation of aldehyde and glycine, offering direct enzymatic synthesis of β-hydroxy-α-amino acids under mild conditions. However, this method suffers from moderate yield and low stereoselectivity at the β-carbon. Given the importance of

A norepinephrine coated magnetic molecularly imprinted polymer for simultaneous multiple chiral recognition.

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A newly designed molecularly imprinted polymer (MIP) material was developed and successfully used as recognition element for enantioselective recognition by microchip electrophoresis. In this work, molecularly imprinted polymers were facilely prepared employing Fe3O4 nanoparticles (NPs) as the

The structure of complement C3b provides insights into complement activation and regulation.

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The human complement system is an important component of innate immunity. Complement-derived products mediate functions contributing to pathogen killing and elimination. However, inappropriate activation of the system contributes to the pathogenesis of immunological and inflammatory diseases.
We describe the design and the use of a circular poly(methyl methacrylate) (PMMA) crystallization platform capable of processing 21 samples in Metal-Assisted and Microwave-Accelerated Evaporative Crystallization (MA-MAEC). The PMMA platforms were modified with silver nanoparticle films (SNFs) to

NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions.

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The hypermodified nucleoside N(6)-threonylcarbamoyladenosine (t(6)A37) is present in many distinct tRNA species and has been found in organisms in all domains of life. This post-transcriptional modification enhances translation fidelity by stabilizing the anticodon/codon interaction in the ribosomal
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