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

Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.

Solid state nuclear magnetic resonance - 1 Jan 2004

Saitô Hazime, Yamaguchi Satoru, Okuda Hideyasu, Shiraishi Aya, Tuzi Satoru

Abstract excerpt

We demonstrate here a general feature of dynamic aspect of membrane proteins as revealed by site-directed 13C NMR studies on bacteriorhodopsin (bR) as a typical membrane protein and a variety of mutants at ambient temperature. 13C NMR signals of [3-13C]Ala- or [1-13C]Val-labeled proteins were assigned regio-specifically with reference to the data of the conformation-dependent 13C chemical shifts from model...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Bacteriorhodopsins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Carbon Isotopes

Share to Lipid Bilayers

Share to Magnetic Resonance Spectroscopy

Share to Membrane Fluidity

Share to Protein Structure, Secondary

Share to Surface Properties

Source

Identifiers

PMID: 14698378
DOI: 10.1016/j.ssnmr.2003.06.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.PMID 14698378Read ↗

Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced by disrupted or disorganized two-dimensional crystalline lattice, through modified lipid-helix and helix-helix interactions, as revealed by 13C NMR.Semantic proximity Read ↗

Cytoplasmic surface structure of bacteriorhodopsin consisting of interhelical loops and C-terminal alpha helix, modified by a variety of environmental factors as studied by (13)C-NMR.Semantic proximity Read ↗

Surface dynamics of bacteriorhodopsin as revealed by (13)C NMR studies on [(13)C]Ala-labeled proteins: detection of millisecond or microsecond motions in interhelical loops and C-terminal alpha-helix.Semantic proximity Read ↗

High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.Semantic proximity Read ↗

Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.Semantic proximity Read ↗

The effect of triple glutamic mutations E9Q/E194Q/E204Q on the structural stability of bacteriorhodopsin.Semantic proximity Read ↗

Functional conformer of c-Myb DNA-binding domain revealed by variable temperature studies.Semantic proximity Read ↗

Probing the flexibility of the bacterial reaction center: the wild-type protein is more rigid than two site-specific mutants.Semantic proximity Read ↗

Solution NMR spectroscopy of [alpha -15N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence.Semantic proximity Read ↗

Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.Semantic proximity Read ↗

Combining high-field EPR with site-directed spin labeling reveals unique information on proteins in action.Semantic proximity Read ↗

Disordered proteins studied by chemical shifts.Semantic proximity Read ↗

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