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1.
Proc Natl Acad Sci U S A ; 116(35): 17316-17322, 2019 08 27.
Artículo en Inglés | MEDLINE | ID: mdl-31409711

RESUMEN

A descendant of the red algal lineage, diatoms are unicellular eukaryotic algae characterized by thylakoid membranes that lack the spatial differentiation of stroma and grana stacks found in green algae and higher plants. While the photophysiology of diatoms has been studied extensively, very little is known about the spatial organization of the multimeric photosynthetic protein complexes within their thylakoid membranes. Here, using cryo-electron tomography, proteomics, and biophysical analyses, we elucidate the macromolecular composition, architecture, and spatial distribution of photosystem II complexes in diatom thylakoid membranes. Structural analyses reveal 2 distinct photosystem II populations: loose clusters of complexes associated with antenna proteins and compact 2D crystalline arrays of dimeric cores. Biophysical measurements reveal only 1 photosystem II functional absorption cross section, suggesting that only the former population is photosynthetically active. The tomographic data indicate that the arrays of photosystem II cores are physically separated from those associated with antenna proteins. We hypothesize that the islands of photosystem cores are repair stations, where photodamaged proteins can be replaced. Our results strongly imply convergent evolution between the red and the green photosynthetic lineages toward spatial segregation of dynamic, functional microdomains of photosystem II supercomplexes.


Asunto(s)
Organismos Acuáticos/enzimología , Proteínas Bacterianas/química , Diatomeas/enzimología , Complejo de Proteína del Fotosistema II/química , Tilacoides/enzimología , Proteínas Bacterianas/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo
2.
Cureus ; 15(7): e42545, 2023 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-37637581

RESUMEN

This retrospective study aimed to assess the effectiveness of continuous glucose monitoring (CGM) devices in managing uncontrolled diabetes mellitus (DM). The study cohort comprised 25 patients with uncontrolled diabetes who received treatment at an internal medicine resident clinic. The objective was to evaluate the impact of transitioning from self-monitoring of blood glucose (SMBG) to CGM devices on glycemic control, as measured by changes in hemoglobin A1c (HbA1c) levels, average blood glucose levels, hypoglycemic events, time spent within the target blood sugar range, and glucose variability. The findings indicated significant improvements in glycemic control with the adoption of CGM devices, highlighting their potential benefits for optimizing diabetes management. The study is particularly interesting because it was done in an internal medicine continuity clinic with the main participation of the internal medicine residents under the supervision of an endocrinologist. It was not done as the majority of the other studies used CGM in specialized endocrinology clinics.

3.
Nat Chem ; 11(7): 605-614, 2019 07.
Artículo en Inglés | MEDLINE | ID: mdl-31209296

RESUMEN

Fractal topologies, which are statistically self-similar over multiple length scales, are pervasive in nature. The recurrence of patterns in fractal-shaped branched objects, such as trees, lungs and sponges, results in a high surface area to volume ratio, which provides key functional advantages including molecular trapping and exchange. Mimicking these topologies in designed protein-based assemblies could provide access to functional biomaterials. Here we describe a computational design approach for the reversible self-assembly of proteins into tunable supramolecular fractal-like topologies in response to phosphorylation. Guided by atomic-resolution models, we develop fusions of Src homology 2 (SH2) domain or a phosphorylatable SH2-binding peptide, respectively, to two symmetric, homo-oligomeric proteins. Mixing the two designed components resulted in a variety of dendritic, hyperbranched and sponge-like topologies that are phosphorylation-dependent and self-similar over three decades (~10 nm-10 µm) of length scale, in agreement with models from multiscale computational simulations. Designed assemblies perform efficient phosphorylation-dependent capture and release of cargo proteins.


Asunto(s)
Proteínas Bacterianas/metabolismo , Fractales , Agregado de Proteínas , Proteínas Recombinantes de Fusión/metabolismo , Algoritmos , Proteínas Bacterianas/genética , Escherichia coli/química , Humanos , Modelos Químicos , Modelos Moleculares , Fosforilación , Ingeniería de Proteínas/métodos , Multimerización de Proteína , Proteínas Recombinantes de Fusión/genética , Dominios Homologos src/genética , Familia-src Quinasas/metabolismo
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