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

Theoretical investigation of infrared spectra and pocket dynamics of photodissociated carbonmonoxy myoglobin.

Biophysical journal - 1 Dec 2003

Nutt David R, Meuwly Markus

Abstract excerpt

Molecular dynamics simulations of the photodissociated state of carbonmonoxy myoglobin (MbCO) are presented using a fluctuating charge model for CO. A new three-point charge model is fitted to high-level ab initio calculations of the dipole and quadrupole moment functions taken from the literature. The infrared spectrum of the CO molecule in the heme pocket is calculated using the dipole moment time...

Read the complete abstract on PubMed

Topics

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

Share to Biophysics
Share to Carbon
Share to Carbon Monoxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Chemical

Share to Myoglobin

Share to Oxygen

Source

Open in PubMed Open full text

Identifiers

PMID: 14645054
DOI: 10.1016/S0006-3495(03)74779-1
PMCID: PMC1303666

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Theoretical investigation of infrared spectra and pocket dynamics of photodissociated carbonmonoxy myoglobin.PMID 14645054Read ↗

Computational infrared and two-dimensional infrared photon echo spectroscopy of both wild-type and double mutant myoglobin-CO proteins.Semantic proximity Read ↗

The effects of the L29F mutation on the ligand migration kinetics in crystallized myoglobin as revealed by molecular dynamics simulations.Semantic proximity Read ↗

An engineered heme-copper center in myoglobin: CO migration and binding.Semantic proximity Read ↗

CO migration in native and mutant myoglobin: atomistic simulations for the understanding of protein function.Semantic proximity Read ↗

Ligand migration and protein fluctuations in myoglobin mutant L29W.Semantic proximity Read ↗

An electrostatic model for the frequency shifts in the carbonmonoxy stretching band of myoglobin: correlation of hydrogen bonding and the stark tuning rate.Semantic proximity Read ↗

Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.Semantic proximity Read ↗

Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities.Semantic proximity Read ↗

Unusually strong H-bonding to the heme ligand and fast geminate recombination dynamics of the carbon monoxide complex of Bacillus subtilis truncated hemoglobin.Semantic proximity Read ↗

Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations.Semantic proximity Read ↗

Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.Semantic proximity Read ↗

Ligand migration in the truncated hemoglobin-II from Mycobacterium tuberculosis: the role of G8 tryptophan.Semantic proximity Read ↗

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