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Structure of the transmembrane cysteine residues in phospholamban
I. T. Arkin
, P. D. Adams
, A. T. Brünger
, S. Aimoto
, D. M. Engelman
, S. O. Smith
*
*
Corresponding author for this work
Research output
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Article
›
peer-review
25
Scopus citations
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Keyphrases
Cysteine Residues
100%
Phospholamban
100%
Transmembrane
100%
Transmembrane Domain
50%
Cysteine
50%
Pentameric Complex
50%
Sulfhydryl Group
50%
Electrostatic Potential
25%
Cardiac muscle Cells
25%
Sarcoplasmic Reticulum
25%
Membrane Protein
25%
Selective Ion
25%
Ion Channels
25%
Ca2+
25%
Hydrogen Bonds (H-bonds)
25%
Side Chain
25%
Carbonyl
25%
Vibrational Spectra
25%
Group Forming
25%
Helix
25%
Mutagenesis Studies
25%
Infrared Spectroscopy
25%
Membrane-active Peptides
25%
Molecular Dynamics Study
25%
Potential Field
25%
Alanine Substitution
25%
Electrostatic Calculations
25%
Polar Side Chain
25%
Biochemistry, Genetics and Molecular Biology
Phospholamban
100%
Cysteine
100%
Transmembrane Domain
50%
Conformation
25%
Dynamics
25%
Cardiac Muscle Cell
25%
Membrane Protein
25%
Wild Type
25%
Mutagenesis
25%
Hydrogen Bond
25%
Electric Potential
25%
Infrared Radiation
25%
Alanine
25%
Ion Channel
25%
Chemistry
Cysteine
100%
Electrostatic Potential
25%
Molecular Dynamics
25%
Hydrogen Bonding
25%
Alanine
25%
Vibrational Spectra
25%