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

Role of rigidity on the activity of proteinase inhibitors and their peptide mimics.

The journal of physical chemistry. B - 28 Sept 2006

Costa Joao R, Yaliraki Sophia N

Abstract excerpt

The Bowman-Birk inhibitors (BBIs) are a family of proteins that share a canonical loop structure whose presence in a conserved conformation is linked to their inhibitory activity. We study the conformational properties of the canonical loop using a graph theoretical approach as implemented in the floppy inclusions and rigid substructure topography (FIRST). We find that the canonical loop is an independent rigid...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Molecular Mimicry
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptides

Share to Protease Inhibitors

Share to Protein Conformation

Source

Identifiers

PMID: 16986893
DOI: 10.1021/jp0575299

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of rigidity on the activity of proteinase inhibitors and their peptide mimics.PMID 16986893Read ↗

KLK4 inhibition by cyclic and acyclic peptides: structural and dynamical insights into standard-mechanism protease inhibitorsSemantic proximity Read ↗

Rigidity, normal modes and flexible motion of a SARS-CoV-2 (COVID-19) protease structureSemantic proximity Read ↗

<i>In Silico</i> Targeting of Calpain-5 in Autosomal Dominant Neovascular Inflammatory Vitreoretinopathy (ADNIV) with Peptides and Natural ProductsSemantic proximity Read ↗

Foci of amino acid residue conservation in the 3D structures of the Kunitz BPTI proteinase inhibitors: how do variants from snake venom differ?Semantic proximity Read ↗

Molecular Dynamics Simulations and Structural Analysis of Giardia duodenalis 14-3-3 Protein–Protein InteractionsSemantic proximity Read ↗

Determination of network of residues that regulate allostery in protein families using sequence analysis.Semantic proximity Read ↗

Decoding Phospho-Regulation and Flanking Regions in Autophagy-Associated Short Linear Motifs: A Case Study of Optineurin-LC3B InteractionSemantic proximity Read ↗

StoneHinge: hinge prediction by network analysis of individual protein structures.Semantic proximity Read ↗

Virtual design for the thermostability enhancement of ketoreductase CgKR1 based on residue interaction network strategy.Semantic proximity Read ↗

Features of protein–protein interactions that translate into potent inhibitors: topology, surface area and affinitySemantic proximity Read ↗

Molecular Dynamics Simulations in Designing DARPins as Phosphorylation-Specific Protein Binders of ERK2.Semantic proximity Read ↗

Conformational flexibility is a critical factor in designing broad-spectrum human norovirus protease inhibitorsSemantic proximity Read ↗

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