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The sweetened actualities of neural membrane proteins: A computational structural analysis

Chauhan et al. | Nov 03, 2022

The sweetened actualities of neural membrane proteins: A computational structural analysis

Here, seeking to better understand the roles of glycans in the receptors of active sites of neuronal cells, the authors used molecular dynamics simulations to to uncover the dynamic nature of N-glycans on membrane proteins. The authors suggest the study of theinteractions of these membrane poreins could provide future potential therapeutic targets to treat mental diseases.

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Association between nonpharmacological interventions and dementia: A retrospective cohort study

Yerabandi et al. | Jan 09, 2023

Association between nonpharmacological interventions and dementia: A retrospective cohort study
Image credit: Ross Sneddon

Here, the authors investigated the role of nonpharmacological interventions in preventing or delaying cognitive impairment in individuals with and without dementia. By using a retrospective case-control study of 22 participants across two senior centers in San Diego, they found no significant differences in self-reported activities. However, they found that their results reflected activity rather than the activity itself, suggesting the need for an alternative type of study.

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Efficacy of Mass Spectrometry Versus 1H Nuclear Magnetic Resonance With Respect to Denaturant Dependent Hydrogen-Deuterium Exchange in Protein Studies

Chenna et al. | Jan 22, 2020

Efficacy of Mass Spectrometry Versus 1H Nuclear Magnetic Resonance With Respect to Denaturant Dependent Hydrogen-Deuterium Exchange in Protein Studies

The misfolding of proteins leads to numerous diseases including Akzheimer’s, Parkinson’s and Type II Diabetes. Understanding of exactly how proteins fold is crucial for many medical advancements. Chenna and Englander addressed this problem by measuring the rate of hydrogen-deuterium exchange within proteins exposed to deuterium oxide in order to further elucidate the process of protein folding. Here, mass spectrometry was used to measure exchange in Cytochrome c and was compared to archived 1H NMR data.

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