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

Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

FEBS letters - 13 Feb 1998

Killick T R, Freund S M, Fersht A R

Abstract excerpt

The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR. Rate constants for changes in individual residues during the unfolding or refolding of the mutants studied by real-time NMR are all...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Mutation
Share to Nuclear Magnetic Resonance, Biomolecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Peptides

Share to Plant Proteins

Share to Protein Folding

Share to Ribonucleases

Share to Time Factors

Source

Identifiers

PMID: 9506851
DOI: 10.1016/s0014-5793(98)00075-1

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.PMID 9506851Read ↗

The kinetic pathway of folding of barnase.Semantic proximity Read ↗

Transient folding intermediates characterized by protein engineering.Semantic proximity Read ↗

Hydrophobic core mutations in CI2 globally perturb fast side-chain dynamics similarly without regard to position.Semantic proximity Read ↗

Submillisecond events in protein folding.Semantic proximity Read ↗

Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography.Semantic proximity Read ↗

Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.Semantic proximity Read ↗

Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy.Semantic proximity Read ↗

Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2.Semantic proximity Read ↗

Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange.Semantic proximity Read ↗

Dynamic spin label study of the barstar-barnase complex.Semantic proximity Read ↗

Ultrafast folding of a computationally designed Trp-cage mutant: Trp2-cage.Semantic proximity Read ↗

13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.Semantic proximity Read ↗

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