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

Submillisecond events in protein folding.

Proceedings of the National Academy of Sciences of the United States of America - 7 Nov 1995

Nölting B, Golbik R, Fersht A R

Abstract excerpt

The pathway of protein folding is now being analyzed at the resolution of individual residues by kinetic measurements on suitably engineered mutants. The kinetic methods generally employed for studying folding are typically limited to the time range of > or = 1 ms because the folding of denatured proteins is usually initiated by mixing them with buffers that favor folding, and the dead time of rapid mixing...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Circular Dichroism
Share to Enzyme Inhibitors

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

Share to Kinetics

Share to Mutation

Share to Protein Denaturation

Share to Protein Folding

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 7479862
DOI: 10.1073/pnas.92.23.10668
PMCID: PMC40673

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

Submillisecond events in protein folding.PMID 7479862Read ↗

Transient folding intermediates characterized by protein engineering.Semantic proximity Read ↗

The kinetic pathway of folding of barnase.Semantic proximity Read ↗

Absolute comparison of simulated and experimental protein-folding dynamics.Semantic proximity Read ↗

Mutational Analysis of Protein Folding Transition States: Phi Values.Semantic proximity Read ↗

Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A.Semantic proximity Read ↗

Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.Semantic proximity Read ↗

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

Microsecond protein folding through a compact transition state.Semantic proximity Read ↗

Experimental assignment of the structure of the transition state for the association of barnase and barstar.Semantic proximity Read ↗

Effect of salt on the urea-unfolded form of barstar probed by m value measurements.Semantic proximity Read ↗

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

Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure.Semantic proximity Read ↗

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