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

Fruitful and futile encounters along the association reaction between proteins.

Biophysical journal - 20 May 2009

Harel Michal, Spaar Alexander, Schreiber Gideon

Abstract excerpt

The association reaction between pairs of proteins proceeds through an encounter complex that develops into the final complex. Here, we combined Brownian dynamics simulations with experimental studies to analyze the structures of the encounter complexes along the association reaction between TEM1-beta-lactamase and its inhibitor, beta-lactamase-inhibitor protein. The encounter complex can be considered as an...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactamase Inhibitors
Share to beta-Lactamases
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Inhibitors

Share to Kinetics

Share to Protein Conformation

Share to Static Electricity

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 19450494
DOI: 10.1016/j.bpj.2009.02.054
PMCID: PMC2712199

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

Fruitful and futile encounters along the association reaction between proteins.PMID 19450494Read ↗

Rational design of faster associating and tighter binding protein complexes.Semantic proximity Read ↗

Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents.Semantic proximity Read ↗

Low-stringency selection of TEM1 for BLIP shows interface plasticity and selection for faster binders.Semantic proximity Read ↗

Barnase-Barstar: from first encounter to final complex.Semantic proximity Read ↗

Promiscuous Protein Binding as a Function of Protein Stability.Semantic proximity Read ↗

Exploring the coupling of dynamic residues in TEM-1 β-lactamase and their role in activity.Semantic proximity Read ↗

Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments.Semantic proximity Read ↗

Mechanisms of protein-ligand association and its modulation by protein mutations.Semantic proximity Read ↗

Binding hot spots in the TEM1-BLIP interface in light of its modular architecture.Semantic proximity Read ↗

The modular architecture of protein-protein binding interfaces.Semantic proximity Read ↗

Molecular dynamics in multidimensional space explains how mutations affect the association path of neomycin to a riboswitch.Semantic proximity Read ↗

The Trajectory Taken by Dimeric Cu/Zn Superoxide Dismutase Through the Protein Unfolding and Dissociation Landscape Is Modulated by Salt-Bridge FormationSemantic proximity Read ↗

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