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

Analyzing pathogenic mutations of C5 domain from cardiac myosin binding protein C through MD simulations.

European biophysics journal : EBJ - 1 Jun 2008

Cecconi Fabio, Guardiani Carlo, Livi Roberto

Abstract excerpt

The folding properties of wild type and mutants of domain C5 from cardiac myosin binding protein C have been investigated via molecular dynamics simulations within the framework of a native-centric and coarse-grained model. The relevance of a mutation has been assessed through the shift in the unfolding temperature, the change in the unfolding rate it determines and Phi-values analysis. In a previous paper...

Read the complete abstract on PubMed

Topics

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

Share to Cardiomyopathy, Hypertrophic, Familial
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Models, Molecular

Share to Protein Denaturation

Share to Protein Folding

Share to Protein Structure, Tertiary

Share to Transition Temperature

Source

Identifiers

PMID: 18379775
DOI: 10.1007/s00249-008-0308-x

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

Analyzing pathogenic mutations of C5 domain from cardiac myosin binding protein C through MD simulations.PMID 18379775Read ↗

Stability and kinetic properties of C5-domain from myosin binding protein C and its mutants.Semantic proximity Read ↗

Computational analysis of folding and mutation properties of C5 domain of myosin binding protein C.Semantic proximity Read ↗

Structure, stability and dynamics of the central domain of cardiac myosin binding protein C (MyBP-C): implications for multidomain assembly and causes for cardiomyopathy.Semantic proximity Read ↗

An Investigation of the Molecular Mechanism of Double cMyBP-C Mutation in a Patient with End-Stage Hypertrophic Cardiomyopathy.Semantic proximity Read ↗

Impact of disease-causing mutations on inter-domain interactions in cMyBP-C: a steered molecular dynamics study.Semantic proximity Read ↗

A coarse-grained mechanical model for folding and unfolding of tropoelastin with possible mutations.Semantic proximity Read ↗

Human cytochrome C natural variants: Studying the membrane binding properties of G41S and Y48H by fluorescence energy transfer and molecular dynamics.Semantic proximity Read ↗

Unveiling the unfolding pathway of F5F8D disorder-associated D81H/V100D mutant of MCFD2 via multiple molecular dynamics simulations.Semantic proximity Read ↗

Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.Semantic proximity Read ↗

Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C.Semantic proximity Read ↗

Molecular Dynamics and Umbrella Sampling Simulations Elucidate Differences in Troponin C Isoform and Mutant Hydrophobic Patch Exposure.Semantic proximity Read ↗

Computational diagnosis of protein conformational diseases: short molecular dynamics simulations reveal a fast unfolding of r-LDL mutants that cause familial hypercholesterolemia.Semantic proximity Read ↗

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