Mutations Pro----Ala-35 and Tyr----Phe-75 of Rhodobacter capsulatus ferrocytochrome c2 affect protein backbone dynamics: measurements of individual amide proton exchange rate constants by 1H-15N HMQC spectroscopy.

doi:10.1021/bi00117a020

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

Back to search

Article

Mutations Pro----Ala-35 and Tyr----Phe-75 of Rhodobacter capsulatus ferrocytochrome c2 affect protein backbone dynamics: measurements of individual amide proton exchange rate constants by 1H-15N HMQC spectroscopy.

Biochemistry - 21 Jan 1992

Gooley P R, Caffrey M S, Cusanovich M A, MacKenzie N E

Abstract excerpt

Comparisons of hydrogen-deuterium solvent exchange rate constants for the NH protons of wild-type Pro----Ala-35 (P35A) and Tyr----Phe-75 (Y75F) Rhodobacter capsulatus ferrocytochromes c2 were made by 1H-15N heteronuclear multiple-quantum correlation spectroscopy. Exchange rate constants increased for the NH protons of residues 45-46, 54, 57-58, 60-61, 82-87, 98, and 100 with Y75F and 16-18, 20, 34, 37, 43, 45-46,...

Topics

Amides
Amino Acid Sequence
Amino Acids
Cytochrome c Group
Cytochromes c2
Deuterium
Hydrogen
Kinetics
Magnetic Resonance Spectroscopy
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nitrogen Isotopes

Oxidation-Reduction

Protein Conformation

Rhodobacter capsulatus

Structure-Activity Relationship

Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 1310038
DOI: 10.1021/bi00117a020

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1310038-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations Pro----Ala-35 and Tyr----Phe-75 of Rhodobacter capsulatus ferrocytochrome c2 affect protein backbone dynamics: measurements of individual amide proton exchange rate constants by 1H-15N HMQC spectroscopy.PMID 1310038Read ↗

Importance of a conserved hydrogen-bonding network in cytochromes c to their redox potentials and stabilities.Semantic proximity Read ↗

Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural differences. A 1H and 15N NMR study.Semantic proximity Read ↗

A spectroscopic analysis of the Pro35----Ala mutant of Rhodobacter capsulatus cytochrome c2. The strictly conserved Pro35 is not structurally essential.Semantic proximity Read ↗

Stability study of Rhodobacter capsulatus ferrocytochrome c2 wild-type and site-directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry.Semantic proximity Read ↗

Probing the influence of mutations on the stability of a ferredoxin by mass spectrometry.Semantic proximity Read ↗

Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.Semantic proximity Read ↗

Five amino acid residues responsible for the high stability of Hydrogenobacter thermophilus cytochrome c552: reciprocal mutation analysis.Semantic proximity Read ↗

Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.Semantic proximity Read ↗

Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants.Semantic proximity Read ↗

Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.Semantic proximity Read ↗

Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.Semantic proximity Read ↗

Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.Semantic proximity Read ↗

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