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

Comparison of C40/82A and P27A C40/82A barstar mutants using 19F NMR.

Biochemistry - 10 Apr 2007

Li Hua, Frieden Carl

Abstract excerpt

Barstar, an inhibitor of the enzyme barnase, contains two phenylalanine residues, three tryptophan residues, and two proline residues. After incorporating either 2-19F-Phe, 4-19F-Phe, or 6-19F-Trp, the structural, dynamic, and folding properties of two mutants (C40/82A, a double mutant, and P27A C40/82A, a triple mutant) were studied by 19F NMR. Experiments were performed as a function of temperature and urea...

Read the complete abstract on PubMed

Topics

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

Share to Hydrophobic and Hydrophilic Interactions
Share to Motion
Share to Nuclear Magnetic Resonance, Biomolecular

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

Share to Phenylalanine

Share to Protein Denaturation

Share to Tryptophan

Share to Ultracentrifugation

Source

Identifiers

PMID: 17371049
DOI: 10.1021/bi6026083

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

Comparison of C40/82A and P27A C40/82A barstar mutants using 19F NMR.PMID 17371049Read ↗

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.Semantic proximity Read ↗

Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase.Semantic proximity Read ↗

The role of Glu73 of barnase in catalysis and the binding of barstar.Semantic proximity Read ↗

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

Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation.Semantic proximity Read ↗

Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure.Semantic proximity Read ↗

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

Effect of salt on the urea-unfolded form of barstar probed by m value measurements.Semantic proximity Read ↗

Structural response to mutation at a protein-protein interface.Semantic proximity Read ↗

Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant.Semantic proximity Read ↗

Backbone dynamics of barstar: a (15)N NMR relaxation study.Semantic proximity Read ↗

Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.Semantic proximity Read ↗

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