Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often involves stepwise establishment of regular secondary and supersecondary structures, namely α-helices and β-sheets, that fold rapidly, stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure.
Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.
Aggregated forms of α-synuclein are characteristic of Parkinson’s disease. Here the authors show that the condensation-driven aggregation pathway of α-synuclein can be inhibited using small molecules: the aminosterol claramine stabilizes α-synuclein condensates and inhibits α-synuclein primary nucleation in the aggregation process.
The aggregation of the neuronal protein α-Synuclein is associated with the onset of Parkinson’s disease. Here the authors report a two-dimensional Fragment Assisted Structure-based technique to find antagonists of α-Synuclein aggregation and show its promise for identifying lead therapeutics for Parkinson’s disease.
A study on cryo-EM structural analysis of AFP, including N-glycosylation, fatty acids, and metal ion binding sites, and a systematic comparison with HSA.
This Perspective discusses the potential of protein structure-prediction models for exploring the structural landscape and specificity of TCR–pMHC interactions.
Pei et al. applied Gaussian process-based machine learning to capture dynamic spatial covariance relationships managed by proteostasis to mediate cooperative folding on a residue basis as a standard model for precision disease management.
Trait correlations impact evolvability as selection on one trait can influence others. Here, the authors examine trait correlation in two proteins, a fluorescent protein & an antibiotic resistance enzyme, observing rapid evolution of trait correlations through changes in the biophysical properties of these proteins.
Claire Durrant reminds us of the importance of studying the physiological roles of proteins and their aggregates to understand their roles in disease and inform therapies, discussing a 2008 paper on amyloid-β from the Arancio lab.
Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.
Cryo-electron microscopy of brain tissue from two individuals with Down syndrome showed amyloid-β (Aβ) and tau filaments identical to those found in individuals with sporadic or dominantly inherited Alzheimer disease (AD), but also two types of Aβ40 filaments with distinct structures different from those previously reported in AD and cerebral amyloid angiopathy.