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

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

Biochemistry - 19 Jan 1993

Matthews S J, Jandu S K, Leatherbarrow R J

Abstract excerpt

Recombinant chymotrypsin inhibitor 2 (CI-2) and the three mutants Ile39-->Val, Ile39-->Leu, and Arg67-->Ala were successfully enriched with [2-13C]tryptophan at position 24 within the hydrophobic core of the protein. Carbon-13 NMR relaxation measurements were then used to investigate the effect o...

Topics

Base Sequence
Carbon Isotopes
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Oligodeoxyribonucleotides
Peptides
Plant Proteins
Protein Folding
Tryptophan

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 8422372
DOI: 10.1021/bi00053a034

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8422372-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.PMID 8422372Read ↗

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

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

Rational Design of Chymotrypsin Inhibitor 2 by Optimizing Non-Native Interactions.Semantic proximity Read ↗

Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions.Semantic proximity Read ↗

Targeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability.Semantic proximity Read ↗

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

In silico mutations and molecular dynamics studies on a winged bean chymotrypsin inhibitor protein.Semantic proximity Read ↗

The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2.Semantic proximity Read ↗

Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.Semantic proximity Read ↗

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

Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability.Semantic proximity Read ↗

Structural determinants of Cys2His2 zinc fingers.Semantic proximity Read ↗

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