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 pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.

Biochemistry - 25 Feb 2003

Smith Christopher R, Wandschneider Eydiejo, Bowler Bruce E

Abstract excerpt

The effect of pH on the denatured state (3 M guanidine hydrochloride) was evaluated with fluorescence spectroscopy for four variants of iso-1-cytochrome c, AcTM (no surface histidines), AcH26 (surface histidine at position 26), AcH54 (surface histidine at position 54), and AcH54I52 (stabilizing I52 mutation added to AcH54). Changes in the compactness and the heme ligation of the denatured state, as a function of...

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 Cytochrome c Group
Share to Cytochromes c

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanidine

Share to Protein Denaturation

Share to Spectrometry, Fluorescence

Share to Tryptophan

Source

Identifiers

PMID: 12590607
DOI: 10.1021/bi026827i

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.PMID 12590607Read ↗

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

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

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

Probing the bottom of a folding funnel using conformationally gated electron transfer reactions.Semantic proximity Read ↗

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

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

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.Semantic proximity Read ↗

Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants.Semantic proximity Read ↗

Role of a highly conserved electrostatic interaction on the surface of cytochrome C in control of the redox function.Semantic proximity Read ↗

Functional role of a protein foldon--an Omega-loop foldon controls the alkaline transition in ferricytochrome c.Semantic proximity Read ↗

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

Stability of the heme Fe-N-terminal amino group coordination bond in denatured cytochrome c.Semantic proximity Read ↗

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