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

Mutational analysis of hydrogen bonding residues in the BPTI folding pathway.

Journal of molecular biology - 26 Oct 2001

Bulaj G, Goldenberg D P

Abstract excerpt

Nine BPTI variants with replacements that remove one or more hydrogen bonds from the native protein were constructed, and the folding pathways of these proteins were determined by isolating and identifying the disulfide-bonded intermediates that accumulated during unfolding and refolding. The forward and reverse rate constants for the individual steps in the folding pathways for each protein were measured,...

Read the complete abstract on PubMed

Topics

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

Share to Aprotinin
Share to Asparagine
Share to Disulfides

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

Share to Dithiothreitol

Share to Hydrogen Bonding

Share to Protein Denaturation

Share to Protein Folding

Share to Thermodynamics

Source

Identifiers

PMID: 11676545
DOI: 10.1006/jmbi.2001.5046

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

Mutational analysis of hydrogen bonding residues in the BPTI folding pathway.PMID 11676545Read ↗

Early events in the disulfide-coupled folding of BPTI.Semantic proximity Read ↗

Phi-values for BPTI folding intermediates and implications for transition state analysis.Semantic proximity Read ↗

Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink.Semantic proximity Read ↗

Hydrophobic interactions accelerate early stages of the folding of BPTI.Semantic proximity Read ↗

Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state.Semantic proximity Read ↗

Effects of amino acid replacements on the reductive unfolding kinetics of pancreatic trypsin inhibitor.Semantic proximity Read ↗

Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds.Semantic proximity Read ↗

Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins.Semantic proximity Read ↗

Stability of the residual structure in unfolded BPTI in different conditions of temperature and solvent composition measured by disulphide kinetics and double mutant cycle analysis.Semantic proximity Read ↗

A mechanism by which binding of the broadly neutralizing antibody b12 unfolds the inner domain α1 helix in an engineered HIV-1 gp120.Semantic proximity Read ↗

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

Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.Semantic proximity Read ↗

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