Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Atomistic folding simulations of the five-helix bundle protein λ(6−85).

Journal of the American Chemical Society - 2 Feb 2011

Bowman Gregory R, Voelz Vincent A, Pande Vijay S

Abstract excerpt

Protein folding is a classic grand challenge that is relevant to numerous human diseases, such as protein misfolding diseases like Alzheimer’s disease. Solving the folding problem will ultimately require a combination of theory, simulation, and experiment, with theory and simulation providing an atomically detailed picture of both the thermodynamics and kinetics of folding and experimental tests grounding these...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacteriophage lambda
Share to Kinetics
Share to Markov Chains

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptide Fragments

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Repressor Proteins

Share to Viral Regulatory and Accessory Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 21174461
DOI: 10.1021/ja106936n
PMCID: PMC3043158

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Atomistic folding simulations of the five-helix bundle protein λ(6−85).PMID 21174461Read ↗

Folding lambda-repressor at its speed limit.Semantic proximity Read ↗

Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions.Semantic proximity Read ↗

The fast and the slow: folding and trapping of λ6-85.Semantic proximity Read ↗

Microsecond protein folding through a compact transition state.Semantic proximity Read ↗

DBFOLD: An efficient algorithm for computing folding pathways of complex proteinsSemantic proximity Read ↗

Variations in the fast folding rates of the lambda-repressor: a hybrid molecular dynamics study.Semantic proximity Read ↗

Energy landscapes for protein foldingSemantic proximity Read ↗

NEXT-FRET: A solution-based smFRET platform to resolve folding intermediates under native conditionsSemantic proximity Read ↗

Experimental snapshots of a protein-DNA binding landscape.Semantic proximity Read ↗

Tuning lambda6-85 towards downhill folding at its melting temperature.Semantic proximity Read ↗

Folding at the speed limit.Semantic proximity Read ↗

Principles of protein folding--a perspective from simple exact models.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.