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

Molecular dynamic simulations of nanomechanic chaperone peptide and effects of in silico His mutations on nanostructured function.

Journal of peptide science : an official publication of the European Peptide Society - 1 Nov 2008

Barzegar Abolfazl, Moosavi-Movahedi Ali Akbar, Mahnam Karim, Bahrami Homayoon, Sheibani Nader

Abstract excerpt

The nanoscale peptide YSGVCHTDLHAWHGDWPLPVK exhibits molecular chaperone activity and prevents protein aggregation under chemical and/or thermal stress. Here, His mutations of this peptide and their impact on chaperone activity were evaluated using theoretical techniques. Molecular dynamic (MD) simulations with simulated annealing (SA) of different mutant nanopeptides were employed to determine the contribution...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Dehydrogenase
Share to Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Chaperones

Share to Molecular Conformation

Share to Nanostructures

Share to Nanotechnology

Share to Proline

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 18683277
DOI: 10.1002/psc.1055

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

Molecular dynamic simulations of nanomechanic chaperone peptide and effects of in silico His mutations on nanostructured function.PMID 18683277Read ↗

The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein.Semantic proximity Read ↗

Factors that drive peptide assembly and fibril formation: experimental and theoretical analysis of Sup35 NNQQNY mutants.Semantic proximity Read ↗

Binding of antigenic peptide to the endoplasmic reticulum-resident protein gp96/GRP94 heat shock chaperone occurs in higher order complexes. Essential role of some aromatic amino acid residues in the peptide-binding site.Semantic proximity Read ↗

Modulation of Mechanical Properties of Short Bioinspired Peptide Materials by Single Amino-Acid Mutations.Semantic proximity Read ↗

Communication: The electrostatic polarization is essential to differentiate the helical propensity in polyalanine mutants.Semantic proximity Read ↗

Backbone-driven collapse in unfolded protein chains.Semantic proximity Read ↗

Packing in protein cores.Semantic proximity Read ↗

Use of constrained synthetic amino acids in beta-helix proteins for conformational control.Semantic proximity Read ↗

Structure propensities in mutated polyglutamine peptides.Semantic proximity Read ↗

Distinction in binding of peptides (P2E) and its mutations (P2G, P2Q) to a graphene sheet via a hierarchical coarse-grained Monte Carlo simulation.Semantic proximity Read ↗

Pore Restructuring of Peptide Frameworks by Mutations at Distal Packing Residues.Semantic proximity Read ↗

Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues.Semantic proximity Read ↗

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