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

Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7.

Proceedings of the National Academy of Sciences of the United States of America - 3 Jan 2006

Gsponer Joerg, Hopearuoho Harri, Whittaker Sara B-M, Spence Graham R, Moore Geoffrey R, Paci Emanuele, Radford Sheena E, Vendruscolo Michele

Abstract excerpt

We present a detailed structural characterization of the intermediate state populated during the folding and unfolding of the bacterial immunity protein Im7. We achieve this result by incorporating a variety of experimental data available for this species in molecular dynamics simulations. First, we define the structure of the exchange-competent intermediate state of Im7 by using equilibrium hydrogen-exchange...

Read the complete abstract on PubMed

Topics

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

Share to Biophysical Phenomena
Share to Biophysics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carrier Proteins

Share to Escherichia coli Proteins

Share to Fluorescence

Share to Protein Conformation

Share to Protein Folding

Share to Spectrum Analysis, Raman

Source

Open in PubMed Open full text

Identifiers

PMID: 16371468
DOI: 10.1073/pnas.0508667102
PMCID: PMC1324994

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

Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7.PMID 16371468Read ↗

Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins.Semantic proximity Read ↗

Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7.Semantic proximity Read ↗

Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.Semantic proximity Read ↗

Im7 folding mechanism: misfolding on a path to the native state.Semantic proximity Read ↗

Trapping the on-pathway folding intermediate of Im7 at equilibrium.Semantic proximity Read ↗

Consequences of localized frustration for the folding mechanism of the IM7 protein.Semantic proximity Read ↗

Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7.Semantic proximity Read ↗

Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Semantic proximity Read ↗

Escherichia coli processivity clamp β from DNA polymerase III is dynamic in solution.Semantic proximity Read ↗

Role of tyrosine hot-spot residues at the interface of colicin E9 and immunity protein 9: a comparative free energy simulation study.Semantic proximity Read ↗

Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation.Semantic proximity Read ↗

Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate.Semantic proximity Read ↗

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