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

Steady state and time resolved effects of guanidine hydrochloride on the structure of Humicola lanuginosa lipase revealed by fluorescence spectroscopy.

Protein science : a publication of the Protein Society - 1 Mar 2000

Zhu K, Jutila A, Kinnunen P K

Abstract excerpt

Effects of guanidine hydrochloride (GdnHCl) on the structure and dynamics of wild-type Humicola lanuginosa lipase (HLL) and its two mutants were studied. The latter were S146A (with the active site Ser replaced by Ala) and the single Trp mutant W89m, with substitutions W117F, W221H, and W260H. Steady-state, stopped-flow, and time-resolved laser-induced fluorescence spectroscopy were carried out as a function of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Ascomycota

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Binding Sites

Share to Guanidine

Share to Lipase

Share to Protein Structure, Tertiary

Share to Spectrometry, Fluorescence

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 10752622
DOI: 10.1110/ps.9.3.598
PMCID: PMC2144562

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Steady state and time resolved effects of guanidine hydrochloride on the structure of Humicola lanuginosa lipase revealed by fluorescence spectroscopy.PMID 10752622Read ↗

Impact of the tryptophan residues of Humicola lanuginosa lipase on its thermal stability.Semantic proximity Read ↗

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

Subdomain-specific collapse of denatured staphylococcal nuclease revealed by single molecule fluorescence resonance energy transfer measurements.Semantic proximity Read ↗

Tryptophan Fluorescence Yields and Lifetimes as a Probe of Conformational Changes in Human Glucokinase.Semantic proximity Read ↗

The effect of mutations in the lid region of Thermomyces lanuginosus lipase on interactions with triglyceride surfaces: A multi-scale simulation study.Semantic proximity Read ↗

Altering the activation mechanism in Thermomyces lanuginosus lipase.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 ↗

The Relation Between Lipase Thermostability and Dynamics of Hydrogen Bond and Hydrogen Bond Network Based on Long Time Molecular Dynamics Simulation.Semantic proximity Read ↗

Elucidation of solvent exposure, side-chain reactivity, and steric demands of the trifluoromethionine residue in a recombinant protein.Semantic proximity Read ↗

Slow solvation dynamics at the active site of an enzyme: implications for catalysis.Semantic proximity Read ↗

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