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

Structural and thermodynamic encoding in the sequence of rat microsomal cytochrome b(5).

Biopolymers - 1 May 2008

Lecomte Juliette T J, Mukhopadhyay Kunal, Pond Matthew P

Abstract excerpt

The water-soluble domain of rat microsomal cytochrome b(5) is a convenient protein with which to inspect the connection between amino acid sequence and thermodynamic properties. In the absence of its single heme cofactor, cytochrome b(5) contains a partially folded stretch of 30 residues. This region is recognized as prone to disorder by programs that analyze primary structures for such intrinsic features. The...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Cytochromes b5
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Microsomes

Share to Molecular Structure

Share to Protein Denaturation

Source

Open in PubMed Open full text

Identifiers

PMID: 18041061
DOI: 10.1002/bip.20892
PMCID: PMC6707728

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

Structural and thermodynamic encoding in the sequence of rat microsomal cytochrome b(5).PMID 18041061Read ↗

Accommodating a nonconservative internal mutation by water-mediated hydrogen bonding between β-sheet strands: a comparison of human and rat type B (mitochondrial) cytochrome b5.Semantic proximity Read ↗

The thermal stability of cytochrome b5.Semantic proximity Read ↗

A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data.Semantic proximity Read ↗

X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35-->Tyr mutant.Semantic proximity Read ↗

The expression of bovine microsomal cytochrome b5 in Escherichia coli and a study of the solution structure and stability of variant proteins.Semantic proximity Read ↗

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

A novel mutation of the cytochrome-b5 reductase gene in an Indian patient: the molecular basis of type I methemoglobinemia.Semantic proximity Read ↗

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

Dissociation of heme from myoglobin and cytochrome b5: comparison of behavior in solution and the gas phase.Semantic proximity Read ↗

Partially formed native tertiary interactions in the A-state of cytochrome c.Semantic proximity Read ↗

Effects of charged amino-acid mutation on the solution structure of cytochrome b(5) and binding between cytochrome b(5) and cytochrome c.Semantic proximity Read ↗

Interfacial hydration, dynamics and electron transfer: multi-scale ET modeling of the transient [myoglobin, cytochrome b5] complex.Semantic proximity Read ↗

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