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

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

Journal of molecular biology - 7 Dec 2001

Lindberg M O, Tångrot J, Otzen D E, Dolgikh D A, Finkelstein A V, Oliveberg M

Abstract excerpt

To examine the influence of contact order and stability on the refolding rate constant for two-state proteins, we have analysed the folding kinetics of the small beta-alpha-beta protein S6 and two of its circular permutants with relative contact orders of 0.19, 0.15 and 0.12. Data reveal a small...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Cyclization
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Engineering

Share to Protein Folding

Share to Proteins

Share to Ribosomal Proteins

Share to Thermodynamics

Source

Identifiers

PMID: 11734005
DOI: 10.1006/jmbi.2001.5186

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11734005-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.PMID 11734005Read ↗

Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state.Semantic proximity Read ↗

Effect of circular permutations on transient partial unfolding in proteins.Semantic proximity Read ↗

Conformational detours during folding of a collapsed state.Semantic proximity Read ↗

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.Semantic proximity Read ↗

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

Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis.Semantic proximity Read ↗

The roles of stability and contact order in determining protein folding rates.Semantic proximity Read ↗

Burst-phase expansion of native protein prior to global unfolding in SDS.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 ↗

Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein.Semantic proximity Read ↗

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

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