Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling.

Julian O Streit^1,2, Michele Invernizzi³, Sandro Bottaro³, Kamil Tamiola³, Kresten Lindorff-Larsen⁴

¹Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark.

²Institute of Structural and Molecular Biology, Department of Structural and Molecular Biology, University College London, London, UK.

³Peptone Switzerland AG, Bellinzona, CH, Switzerland.

⁴Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark. lindorff@bio.ku.dk.

PubMed PMC DOI PDF

Abstract

Intrinsically disordered proteins populate heterogeneous conformational ensembles that are challenging to characterise. While all-atom molecular dynamics simulations can provide detailed insights into dynamic ensembles, achieving sufficient sampling remains difficult. Here, we show that On-the-fly Probability Enhanced Sampling (OPES) in the multithermal ensemble enables efficient generation of ato…

Create a free account to keep reading

Free members get 10 full research views every month across publications, clinical trials, FDA clearances, adverse events, and NIH grants. No credit card required.

Create Free Account Sign In

Want unlimited research access? See Pro plans

Data Accuracy Notice: Research intelligence on Health AI Central is aggregated from public sources (PubMed, ClinicalTrials.gov, FDA, NIH, CMS, and others) and refreshed nightly. Classifications and derived metrics are produced by automated methods described in our Methodology. We recommend verifying critical data points against the primary sources before making decisions.