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

Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.

Proceedings of the National Academy of Sciences of the United States of America - 5 Jun 2007

Sato Akira, Gao Ying, Kitagawa Teizo, Mizutani Yasuhisa

Abstract excerpt

Time-resolved UV resonance Raman (UVRR) spectroscopic studies of WT and mutant myoglobin were performed to reveal the dynamics of protein motion after ligand dissociation. After dissociation of carbon monoxide (CO) from the heme, UVRR bands of Tyr showed a decrease in intensity with a time constant of 2 ps. The intensity decrease was followed by intensity recovery with a time constant of 8 ps. On the other hand,...

Read the complete abstract on PubMed

Topics

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

Share to Carbon Monoxide
Share to Ligands
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Myoglobin

Share to Photochemistry

Share to Protein Conformation

Share to Spectrum Analysis, Raman

Source

Open in PubMed Open full text

Identifiers

PMID: 17517618
DOI: 10.1073/pnas.0611560104
PMCID: PMC1887578

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.PMID 17517618Read ↗

Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF.Semantic proximity Read ↗

Ligand-induced protein responses and mechanical signal propagation described by linear response theories.Semantic proximity Read ↗

Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy.Semantic proximity Read ↗

Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme 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 ↗

Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain.Semantic proximity Read ↗

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

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

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

Ligand pathways in myoglobin: a review of Trp cavity mutations.Semantic proximity Read ↗

Structural dynamics of myoglobin.Semantic proximity Read ↗

Effect of Occluded Ligand Migration on the Kinetics and Structural Dynamics of Homodimeric Hemoglobin.Semantic proximity Read ↗

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