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

NMR Spectroscopic Studies Reveal the Critical Role of the Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

Biochemistry - 23 Jun 2020

Zhang Nan, Liu Jing, Liu Yajie, Wu Wen-Hao, Fang Jing, Da Xiao-Di, Wang Shenlin, Zhang Wen-Bin

Abstract excerpt

The interplay between protein folding and chemical reaction has been an intriguing subject. In this contribution, we report the study of SpyTag and SpyCatcher reactive mutants using a combination of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, liquid chromatography and mass spectrometry, circular dichroism, and NMR spectroscopy. It was found that the wild-type SpyCatcher is well-folded in solution...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Cyclization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Peptides

Share to Protein Stability

Source

Identifiers

PMID: 32469203
DOI: 10.1021/acs.biochem.0c00287

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NMR Spectroscopic Studies Reveal the Critical Role of the Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.PMID 32469203Read ↗

In Silico Screening Using Freely Available Computational Tools to Generate Novel Peptide/Protein Pairs for Protein-Protein Ligation.Semantic proximity Read ↗

One-step purification and immobilization of recombinant proteins using SpyTag/SpyCatcher chemistry.Semantic proximity Read ↗

pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate.Semantic proximity Read ↗

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.Semantic proximity Read ↗

Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a non-phosphorylatable active-site mutant of the 128 kDa enzyme I dimer.Semantic proximity Read ↗

Tailoring protein nanomechanics with chemical reactivity.Semantic proximity Read ↗

Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.Semantic proximity Read ↗

Solution structure of proinsulin: connecting domain flexibility and prohormone processing.Semantic proximity Read ↗

Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys-->Ser mutant proteins.Semantic proximity Read ↗

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium.Semantic proximity Read ↗

Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway.Semantic proximity Read ↗

NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms.Semantic proximity Read ↗

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