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1.
Opt Lett ; 42(6): 1084-1087, 2017 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-28295098

RESUMO

The large-scale and low-cost fabrication of high sensitivity sensors for the real-time detection of biochemicals and molecular substances opens up new opportunities in the areas of bioanalytic screening and medical diagnostics. Planar integrated photonic resonators that can be fabricated with a low footprint, in spatial and wavelength multiplexed arrangements, and that enable integration with microfluidics on the wafer scale have emerged as a promising sensing platform for these application fields. We realized an optofluidic and label-free biosensor that is based on hydrogenated amorphous silicon microring resonators embedded in silicon/glass microfluidic channels for analyte injection and biomolecule immobilization. The optofluidic sensor merits for refractive index and biomolecule sensing are evaluated by sensitivity and detection limit simulations, whereas a proof of concept is demonstrated by real-time protein immobilization experiments of functionalized resonators.

2.
Cell Mol Life Sci ; 59(3): 513-8, 2002 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-11964128

RESUMO

The most alkaline form of pectin methylesterase was purified from ripe carrot roots and used for structural analysis. Determination of an N-terminal blocking group and of the primary structure allowed comparisons with other forms, and facilitated crystallographic determination of the three-dimensional structure. The mature enzyme has 319 residues and the N-terminal blocking group was shown to be a pyroglutamyl residue derived from a glutaminyl cyclization. Few other methylesterases have been isolated and assigned to exact mature forms, and together with the present enzyme, only two have been analyzed in three-dimensional structure. However, comparison of 39 forms, mainly from GenBank data, reveals clear relationships and identifies subgroups of this enzyme type, deviating in structure but centering around two functionally important and conserved Asp residues at positions 136 and 157 in the carrot enzyme.


Assuntos
Hidrolases de Éster Carboxílico/química , Hidrolases de Éster Carboxílico/metabolismo , Daucus carota/enzimologia , Sequência de Aminoácidos , Ácido Aspártico/metabolismo , Sítios de Ligação , Dados de Sequência Molecular , Homologia de Sequência de Aminoácidos , Relação Estrutura-Atividade
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