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

Unfolding of the cold shock protein studied with biased molecular dynamics.

Proteins - 15 Nov 2003

Morra Giulia, Hodoscek Milan, Knapp Ernst-Walter

Abstract excerpt

The cold shock protein from Bacillus caldolyticus is a small beta-barrel protein that folds in a two-state mechanism. For the native protein and for several mutants, a wealth of experimental data are available on stability and folding, so that it is an optimal system to study this process. We compare data from unfolding simulations (trajectories of 5 and up to 12 ns) obtained with a bias potential at room...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Computer Simulation
Share to Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Models, Molecular

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Temperature

Source

Identifiers

PMID: 14579351
DOI: 10.1002/prot.10344

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unfolding of the cold shock protein studied with biased molecular dynamics.PMID 14579351Read ↗

Role of electrostatic interactions for the stability and folding behavior of cold shock protein.Semantic proximity Read ↗

Electrostatic stabilization of a thermophilic cold shock protein.Semantic proximity Read ↗

Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model.Semantic proximity Read ↗

Key role of coulombic interactions for the folding transition state of the cold shock protein.Semantic proximity Read ↗

Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability.Semantic proximity Read ↗

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.Semantic proximity Read ↗

Electrostatic contributions to the stability of a thermophilic cold shock protein.Semantic proximity Read ↗

Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions.Semantic proximity Read ↗

Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability.Semantic proximity Read ↗

Two exposed amino acid residues confer thermostability on a cold shock protein.Semantic proximity Read ↗

Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling.Semantic proximity Read ↗

Free-energy landscapes of membrane co-translocational protein unfolding.Semantic proximity Read ↗

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