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

Structural consequences of an amino acid deletion in the B1 domain of protein G.

Proteins - 15 Nov 2000

O'Neil K T, Bach A C, DeGrado W F

Abstract excerpt

We describe the NMR structure of a deletion mutant of the B1 IgG-binding domain from Group G Streptococcus. The deletion occurs within the last beta-strand of the protein, where it may potentially have a deleterious effect on the stability of the protein if the protein were not able to conformationally adjust to the perturbation. In particular, the deletion changes the registry of the final three residues in the...

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 Motion
Share to Nuclear Magnetic Resonance, Biomolecular

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

Share to Peptide Fragments

Share to Protein Structure, Secondary

Share to Receptors, IgG

Share to Solutions

Share to Thermodynamics

Source

Identifiers

PMID: 11025544
DOI: 10.1002/1097-0134(20001115)41:3<323::aid-prot50>3.0.co;2-r

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

Structural consequences of an amino acid deletion in the B1 domain of protein G.PMID 11025544Read ↗

A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping.Semantic proximity Read ↗

Core mutations switch monomeric protein GB1 into an intertwined tetramer.Semantic proximity Read ↗

Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.Semantic proximity Read ↗

Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution.Semantic proximity Read ↗

The design and characterization of two proteins with 88% sequence identity but different structure and function.Semantic proximity Read ↗

NMR-detected conformational exchange observed in a computationally designed variant of protein Gbeta1.Semantic proximity Read ↗

Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin.Semantic proximity Read ↗

Deciphering GB1’s Single Mutational Landscape: Insights from MuMi AnalysisSemantic proximity Read ↗

Critical role of beta-hairpin formation in protein G folding.Semantic proximity Read ↗

A tale of two secondary structure elements: when a beta-hairpin becomes an alpha-helix.Semantic proximity Read ↗

pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability.Semantic proximity Read ↗

Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.Semantic proximity Read ↗

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