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

The role of domain: domain interactions versus domain: water interactions in the coarse-grained simulations of the E1P to E2P transitions in Ca-ATPase (SERCA).

Proteins - 1 Aug 2012

Nagarajan Anu, Andersen Jens Peter, Woolf Thomas B

Abstract excerpt

SERCA is an important model system for understanding the molecular details of conformational change in membrane transport systems. This reflects the large number of solved X-ray structures and the equally large database of mutations that have been assayed. In this computational study, we provide a molecular dynamics description of the conformational changes during the E1P → E2P transitions. This set of states...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Hydrogen Bonding
Share to Lipids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Protein Interaction Domains and Motifs

Share to Rabbits

Share to Sarcoplasmic Reticulum Calcium-Transporting ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 22422644
DOI: 10.1002/prot.24070
PMCID: PMC3388165

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

The role of domain: domain interactions versus domain: water interactions in the coarse-grained simulations of the E1P to E2P transitions in Ca-ATPase (SERCA).PMID 22422644Read ↗

Coarse-grained simulations of transitions in the E2-to-E1 conformations for Ca ATPase (SERCA) show entropy-enthalpy compensation.Semantic proximity Read ↗

Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.Semantic proximity Read ↗

Relationship between Ca2+-affinity and shielding of bulk water in the Ca2+-pump from molecular dynamics simulations.Semantic proximity Read ↗

Three key residues form a critical contact network in a protein folding transition state.Semantic proximity Read ↗

Interconversion of functional motions between mesophilic and thermophilic adenylate kinases.Semantic proximity Read ↗

Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation- <i>π</i> contacts in proteinsSemantic proximity Read ↗

Roles of long-range electrostatic domain interactions and K+ in phosphoenzyme transition of Ca2+-ATPase.Semantic proximity Read ↗

Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca2+-ATPase.Semantic proximity Read ↗

Molecular Dynamics Simulations of Orai Reveal How the Third Transmembrane Segment Contributes to Hydration and Ca2+ Selectivity in Calcium Release-Activated Calcium Channels.Semantic proximity Read ↗

Interaction between the catalytic site and the A-M3 linker stabilizes E2/E2P conformational states of Na+,K+-ATPase.Semantic proximity Read ↗

Counterion-assisted cation transport in a biological calcium channel.Semantic proximity Read ↗

Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.Semantic proximity Read ↗

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