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

Effect of circular permutations on transient partial unfolding in proteins.

Protein science : a publication of the Protein Society - 1 Aug 2016

Chen Chen, Yun Jung-Hun, Kim Jae-Hoon, Park Chiwook

Abstract excerpt

Under native conditions, proteins can undergo transient partial unfolding, which may cause proteins to misfold or aggregate. A change in sequence connectivity by circular permutation may affect the energetics of transient partial unfolding in proteins without altering the three-dimensional structures. Using Escherichia coli dihydrofolate reductase (DHFR) as a model system, we investigated how circular permutation...

Read the complete abstract on PubMed

Topics

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

Share to Protein Domains
Share to Protein Engineering
Share to Protein Folding

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

Share to Protein Unfolding

Share to Proteolysis

Share to Tetrahydrofolate Dehydrogenase

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 27164316
DOI: 10.1002/pro.2945
PMCID: PMC4972204

Genes

DHFR

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

Effect of circular permutations on transient partial unfolding in proteins.PMID 27164316Read ↗

Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment.Semantic proximity Read ↗

Probing the interactions between the folding elements early in the folding of Escherichia coli dihydrofolate reductase by systematic sequence perturbation analysis.Semantic proximity Read ↗

Systematic circular permutation of an entire protein reveals essential folding elements.Semantic proximity Read ↗

The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.Semantic proximity Read ↗

Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.Semantic proximity Read ↗

Circular permutation in proteins.Semantic proximity Read ↗

Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways.Semantic proximity Read ↗

A rewired green fluorescent protein: folding and function in a nonsequential, noncircular GFP permutant.Semantic proximity Read ↗

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.Semantic proximity Read ↗

Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity.Semantic proximity Read ↗

Stabilization of native protein fold by intein-mediated covalent cyclization.Semantic proximity Read ↗

Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor.Semantic proximity Read ↗

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