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

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

Biophysical journal - 6 Jan 2015

Maeno Akihiro, Sindhikara Daniel, Hirata Fumio, Otten Renee, Dahlquist Frederick W, Yokoyama Shigeyuki, Akasaka Kazuyuki, Mulder Frans A A, Kitahara Ryo

Abstract excerpt

Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins are manifested by their corresponding amino acid sequences, the natural rules for molecular design and their corresponding interplay remain obscure. In this study, we focused on the role of internal cavities of proteins in conformational dynamics. We investigated the pressure-induced responses from the...

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 Carbon Isotopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Muramidase

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Pressure

Share to Proton Magnetic Resonance Spectroscopy

Source

Open in PubMed Open full text

Identifiers

PMID: 25564860
DOI: 10.1016/j.bpj.2014.11.012
PMCID: PMC4286597

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme.PMID 25564860Read ↗

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

Filling a cavity dramatically increases pressure stability of the c-Myb R2 subdomain.Semantic proximity Read ↗

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

The consequences of cavity creation on the folding landscape of a repeat protein depend upon context.Semantic proximity Read ↗

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

The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.Semantic proximity Read ↗

Elucidation of the relationship between enzyme activity and internal motion using a lysozyme stabilized by cavity-filling mutations.Semantic proximity Read ↗

Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin.Semantic proximity Read ↗

Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.Semantic proximity Read ↗

Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.Semantic proximity Read ↗

Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A.Semantic proximity Read ↗

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