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

High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.

Proceedings of the National Academy of Sciences of the United States of America - 25 Jan 2011

McCoy John, Hubbell Wayne L

Abstract excerpt

Identifying equilibrium conformational exchange and characterizing conformational substates is essential for elucidating mechanisms of function in proteins. Site-directed spin labeling has previously been employed to detect conformational changes triggered by some event, but verifying conformatio...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophage T4
Share to Crystallography, X-Ray
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muramidase

Share to Pressure

Share to Protein Unfolding

Share to Spin Labels

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 21205903
DOI: 10.1073/pnas.1017877108
PMCID: PMC3029758

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21205903-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.PMID 21205903Read ↗

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

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

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

Ion Channel Conformation and Oligomerization Assessment by Site-Directed Spin Labeling and Pulsed-EPR.Semantic proximity Read ↗

Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme.Semantic proximity Read ↗

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

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

Using CEST NMR to discover previously unobserved states on the free energy surface of proteins: Application to the L99A cavity mutant of T4 lysozyme.Semantic proximity Read ↗

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

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

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function.Semantic proximity Read ↗

Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): a study of doubly-spin-labeled T4 lysozyme.Semantic proximity Read ↗

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