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

Observing lysozyme's closing and opening motions by high-resolution single-molecule enzymology.

ACS chemical biology - 19 Jun 2015

Akhterov Maxim V, Choi Yongki, Olsen Tivoli J, Sims Patrick C, Iftikhar Mariam, Gul O Tolga, Corso Brad L, Weiss Gregory A, Collins Philip G

Abstract excerpt

Single-molecule techniques can monitor the kinetics of transitions between enzyme open and closed conformations, but such methods usually lack the resolution to observe the underlying transition pathway or intermediate conformational dynamics. We have used a 1 MHz bandwidth carbon nanotube transistor to electronically monitor single molecules of the enzyme T4 lysozyme as it processes substrate. An experimental...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Bacteriophage T4

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Molecular Dynamics Simulation

Share to Motion

Share to Muramidase

Share to Protein Structure, Secondary

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 25763461
DOI: 10.1021/cb500750v
PMCID: PMC4916960

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

Observing lysozyme's closing and opening motions by high-resolution single-molecule enzymology.PMID 25763461Read ↗

Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra-protein switchable motion.Semantic proximity Read ↗

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

Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA.Semantic proximity Read ↗

Direct observation of Thermomyces lanuginosus lipase diffusional states by Single Particle Tracking and their remodeling by mutations and inhibition.Semantic proximity Read ↗

Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.Semantic proximity Read ↗

Automated Path Searching Reveals the Mechanism of Hydrolysis Enhancement by T4 Lysozyme Mutants.Semantic proximity Read ↗

The time scale of the catalytic loop motion in triosephosphate isomerase.Semantic proximity Read ↗

Single-Particle Tracking of Thermomyces lanuginosus Lipase Reveals How Mutations in the Lid Region Remodel Its Diffusion.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 ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.Semantic proximity Read ↗

In cellulo FRET-FLIM and single molecule tracking reveal the supra-molecular organization of the pyoverdine bio-synthetic enzymes in Pseudomonas aeruginosa.Semantic proximity Read ↗

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