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

Conformational Mobility in Cytochrome P450 3A4 Explored by Pressure-Perturbation EPR Spectroscopy.

Biophysical journal - 12 Apr 2016

Davydov Dmitri R, Yang Zhongyu, Davydova Nadezhda, Halpert James R, Hubbell Wayne L

Abstract excerpt

We used high hydrostatic pressure as a tool for exploring the conformational landscape of human cytochrome P450 3A4 (CYP3A4) by electron paramagnetic resonance and fluorescence spectroscopy. Site-directed incorporation of a luminescence resonance energy transfer donor-acceptor pair allowed us to identify a pressure-dependent equilibrium between two states of the enzyme, where an increase in pressure increased the...

Read the complete abstract on PubMed

Topics

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

Share to Cytochrome P-450 CYP3A
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Dyes

Share to Models, Molecular

Share to Mutation

Share to Pressure

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 27074675
DOI: 10.1016/j.bpj.2016.02.026
PMCID: PMC4833771

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational Mobility in Cytochrome P450 3A4 Explored by Pressure-Perturbation EPR Spectroscopy.PMID 27074675Read ↗

High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.Semantic proximity Read ↗

Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.Semantic proximity Read ↗

Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A.Semantic proximity Read ↗

Pressure effects on protein flexibility monomeric proteins.Semantic proximity Read ↗

Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants.Semantic proximity Read ↗

Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR.Semantic proximity Read ↗

Formation of transient oxygen complexes of cytochrome p450 BM3 and nitric oxide synthase under high pressure.Semantic proximity Read ↗

The role of conformational heterogeneity in regulating the apoptotic activity of BAX protein.Semantic proximity Read ↗

Molecular determinants of expansivity of native globular proteins: a pressure perturbation calorimetry study.Semantic proximity Read ↗

Pressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach.Semantic proximity Read ↗

Extensively hydrated but folded: a novel state of globular proteins stabilized at high pressure and low temperature.Semantic proximity Read ↗

Temperature and pressure effects on GFP mutants: explaining spectral changes by molecular dynamics simulations and TD-DFT calculations.Semantic proximity Read ↗

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