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

Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.

Biochemistry - 18 Mar 2003

Desamero Ruel, Rozovsky Sharon, Zhadin Nick, McDermott Ann, Callender Robert

Abstract excerpt

As for many enzymes, the enzymatic pathway of triosephosphate isomerase (TIM) includes the partially rate determining motion of an active site loop (loop 6, residues 166-176), which must remain closed during chemistry but must open just before product release. The motion of this loop was monitored using laser induced temperature-jump relaxation spectroscopy at nanosecond to millisecond time resolution. Trp168 in...

Read the complete abstract on PubMed

Topics

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

Share to Glycerophosphates
Share to Hot Temperature
Share to Models, Chemical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Motion

Share to Spectrometry, Fluorescence

Share to Spectrum Analysis

Share to Thermodynamics

Share to Triose-Phosphate Isomerase

Source

Identifiers

PMID: 12627960
DOI: 10.1021/bi026994i

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

Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.PMID 12627960Read ↗

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

Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.Semantic proximity Read ↗

Dynamic requirements for a functional protein hinge.Semantic proximity Read ↗

Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase.Semantic proximity Read ↗

Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.Semantic proximity Read ↗

Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.Semantic proximity Read ↗

The folding pathway of glycosomal triosephosphate isomerase: structural insights into equilibrium intermediates.Semantic proximity Read ↗

NEXT-FRET: A solution-based smFRET platform to resolve folding intermediates under native conditionsSemantic proximity Read ↗

Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM.Semantic proximity Read ↗

Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.Semantic proximity Read ↗

A strategy based on thermal flexibility to design triosephosphate isomerase proteins with increased or decreased kinetic stability.Semantic proximity Read ↗

Substrate-induced conformational changes in the membrane-embedded IIC(mtl)-domain of the mannitol permease from Escherichia coli, EnzymeII(mtl), probed by tryptophan phosphorescence spectroscopy.Semantic proximity Read ↗

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