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

The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 beta-lactamase is the trans to cis isomerization of a non-proline peptide bond.

Proteins - 1 May 1996

Vanhove M, Raquet X, Palzkill T, Pain R H, Frère J M

Abstract excerpt

The stability and kinetics of unfolding and refolding of the P167T mutant of the TEM-1 beta-lactamase have been investigated as a function of guanidine hydrochloride concentration. The activity of the mutant enzyme was not significantly modified, which strongly suggests that the Glu166-Thr167 pep...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to Enzyme Stability
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Protein Folding

Share to Thermodynamics

Source

Identifiers

PMID: 8727322
DOI: 10.1002/(SICI)1097-0134(199605)25:1<104::AID-PROT8>3.0.CO;2-J

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8727322-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 beta-lactamase is the trans to cis isomerization of a non-proline peptide bond.PMID 8727322Read ↗

Kinetic and thermodynamic consequences of the removal of the Cys-77-Cys-123 disulphide bond for the folding of TEM-1 beta-lactamase.Semantic proximity Read ↗

TEM-1 beta-lactamase folds in a nonhierarchical manner with transient non-native interactions involving the C-terminal region.Semantic proximity Read ↗

Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp.Semantic proximity Read ↗

A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.Semantic proximity Read ↗

A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein.Semantic proximity Read ↗

Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis.Semantic proximity Read ↗

Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis-proline 39 by alanine.Semantic proximity Read ↗

Evidence from a mutant beta-lactamase for the mechanism of beta-lactamase-catalysed depsipeptide aminolysis.Semantic proximity Read ↗

Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1.Semantic proximity Read ↗

pK(a) calculations for class C beta-lactamases: the role of Tyr-150.Semantic proximity Read ↗

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