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

Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.

Journal of molecular biology - 11 Feb 2000

Godbole S, Hammack B, Bowler B E

Abstract excerpt

The changes in the free energy of the denatured state of a set of yeast iso-1-cytochrome c variants with single surface histidine residues have been measured in 3 M guanidine hydrochloride. The thermodynamics of unfolding by guanidine hydrochloride is also reported. All variants have decreased stability relative to the wild-type protein. The free energy of the denatured state was determined in 3 M guanidine...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to Biopolymers
Share to Cytochrome c Group

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

Share to Cytochromes c

Share to Guanidine

Share to Protein Denaturation

Share to Titrimetry

Source

Identifiers

PMID: 10656828
DOI: 10.1006/jmbi.1999.3454

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

Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.PMID 10656828Read ↗

Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.Semantic proximity Read ↗

Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.Semantic proximity Read ↗

The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: investigation of aliphatic residues.Semantic proximity Read ↗

Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Semantic proximity Read ↗

Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.Semantic proximity Read ↗

Rational design of a more stable yeast iso-1-cytochrome c.Semantic proximity Read ↗

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

Changing the transition state for protein (Un) folding.Semantic proximity Read ↗

Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Semantic proximity Read ↗

Unspecific hydrophobic stabilization of folding transition states.Semantic proximity Read ↗

Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.Semantic proximity Read ↗

TEM-1 beta-lactamase folds in a nonhierarchical manner with transient non-native interactions involving the C-terminal region.Semantic proximity Read ↗

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