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potassium channels - chemistry (190) 190
kcsa potassium channel (140) 140
potassium channel (139) 139
protein conformation (131) 131
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potassium channels - metabolism (126) 126
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article (81) 81
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lipids (65) 65
potassium - metabolism (63) 63
multidisciplinary sciences (62) 62
potassium channel kcsa (60) 60
potassium channels - genetics (59) 59
streptomyces-lividans (59) 59
thermodynamics (59) 59
molecular sequence data (57) 57
activation (55) 55
pore (55) 55
research (54) 54
escherichia-coli (53) 53
water (52) 52
dynamics (51) 51
protein binding (51) 51
protein structure, secondary (51) 51
ion channel gating - physiology (47) 47
molecular dynamics simulation (47) 47
bacterial proteins - genetics (46) 46
full-length kcsa (46) 46
kinetics (45) 45
brownian dynamics (44) 44
ion channels - chemistry (44) 44
membrane proteins - chemistry (44) 44
mutation (43) 43
models, biological (42) 42
physiology (42) 42
chemistry, multidisciplinary (41) 41
protein structure, tertiary (41) 41
physiological aspects (40) 40
potassium channels - physiology (40) 40
crystallography, x-ray (39) 39
static electricity (39) 39
channels (38) 38
models (38) 38
physics, atomic, molecular & chemical (38) 38
simulations (38) 38
ion channel (37) 37
kcsa channel (37) 37
models, chemical (37) 37
potassium - chemistry (37) 37
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simulation (36) 36
inactivation (35) 35
lipid bilayers - chemistry (35) 35
binding (34) 34
solid-state nmr (34) 34
structure (34) 34
biological sciences (33) 33
structure-activity relationship (33) 33
water - chemistry (33) 33
molecular biology (32) 32
electrophysiology (31) 31
structural basis (31) 31
ion transport (30) 30
ligands (30) 30
crystal structure (29) 29
k+-channel (29) 29
potassium-channel (29) 29
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1. Full Text Lipid–protein nanodiscs promote in vitro folding of transmembrane domains of multi-helical and multimeric membrane proteins
by Shenkarev, Zakhar O and Lyukmanova, Ekaterina N and Butenko, Ivan O and Petrovskaya, Lada E and Paramonov, Alexander S and Shulepko, Mikhail A and Nekrasova, Oksana V and Kirpichnikov, Mikhail P and Arseniev, Alexander S
BBA - Biomembranes, ISSN 0005-2736, 02/2013, Volume 1828, Issue 2, pp. 776 - 784
Production of helical integral membrane proteins (IMPs) in a folded state is a necessary prerequisite for their functional and structural studies. In many... 
Membrane protein folding | Reconstructed high-density lipoprotein | Bacteriorhodopsin ESR | Potassium channel KcsA | Membrane mimetic | Cell-free expression | PHOSPHOLIPID-BILAYER NANODISCS | FULL-LENGTH KCSA | BIOCHEMISTRY & MOLECULAR BIOLOGY | KCSA POTASSIUM CHANNEL | DETERGENT MICELLES | DENATURED STATE | NMR | BIOPHYSICS | NANOLIPOPROTEIN PARTICLES | K+ CHANNEL | BACTERIORHODOPSIN | EXPRESSION | Protein Structure, Tertiary | Bacteria - metabolism | Protein Structure, Secondary | Detergents - chemistry | Nanotechnology - methods | Streptomyces lividans - metabolism | Bacterial Proteins - chemistry | Phosphatidylcholines - chemistry | Lipids - chemistry | Phosphatidylglycerols - chemistry | Membrane Proteins - chemistry | Sodium Dodecyl Sulfate - chemistry | Bacteriorhodopsins - metabolism | Nanostructures - chemistry | Potassium Channels - chemistry | Cell Membrane - metabolism | Membrane Proteins - metabolism | Proteins - chemistry | Dimerization | Dimyristoylphosphatidylcholine - chemistry | Bacteriorhodopsin | Lipids | Rhodopsin | Surface active agents | Sulfates | Aquaporins
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2. Full Text Electrostatic state of the cytoplasmic domain influences inactivation at the selectivity filter of the KcsA potassium channel
by Hirano, Minako and Ide, Toru
BBA - Biomembranes, ISSN 0005-2736, 01/2019, Volume 1861, Issue 1, pp. 220 - 227
KcsA is a proton-activated K channel that is regulated at two gates: an activation gate located in the inner entrance of the pore and an inactivation gate at... 
Inactivation | KcsA | Potassium channel | TETRAMERIZATION | VOLTAGE | ACTIVATION | FULL-LENGTH KCSA | C-TYPE INACTIVATION | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR DETERMINANTS | BIOPHYSICS | STRUCTURAL BASIS | PORE | K+ CHANNELS | Amino acids | Potassium channels
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3. Full Text Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
by van den Brink-van der Laan, Els and Antoinette Killian, J and de Kruijff, Ben
BBA - Biomembranes, ISSN 0005-2736, 2004, Volume 1666, Issue 1, pp. 275 - 288
Nonbilayer lipids can be defined as cone-shaped lipids with a preference for nonbilayer structures with a negative curvature, such as the hexagonal phase. All... 
Phosphatidylethanolamine | Lipid polymorphism | KcsA | Leader Peptidase | Nonlamellar lipid | Oligomer | Ion channel | Protein–lipid interaction | Curvature | Protein-lipid interaction | lipid polymorphism | ACHOLEPLASMA-LAIDLAWII MEMBRANES | POLYMORPHIC PHASE-BEHAVIOR | MOLECULAR-DYNAMICS | FORMING LIPIDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | oligomer | curvature | leader peptidase | nonlamellar lipid | phosphatidylethanolamine | BIOPHYSICS | RED-CELL MEMBRANE | protein-lipid interaction | ion channel | COLI LEADER PEPTIDASE | K+ CHANNEL | POTASSIUM CHANNEL KCSA | ABC-TRANSPORT-SYSTEM
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4. Full Text Constitutive boost of a K + channel via inherent bilayer tension and a unique tension-dependent modality
by Iwamoto, Masayuki and Oiki, Shigetoshi
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 51, pp. 13117 - 13122
Molecular mechanisms underlying channel-membrane interplay have been extensively studied. Cholesterol, as a major component of the cell membrane, participates... 
Stretch-activated channel | KcsA channel | Contact bubble bilayer | Single-channel | Bilayer tension | Current | MULTIDISCIPLINARY SCIENCES | SENSITIVITY | RECEPTOR | KCSA POTASSIUM CHANNEL | stretch-activated channel | single-channel current | CAPACITANCE | bilayer tension | LIPID-BILAYERS | MECHANOSENSITIVE CHANNEL | ION-CHANNEL | DYNAMICS | MEMBRANE CHOLESTEROL | contact bubble bilayer | BINDING | Cell Membrane - chemistry | Potassium Channels - metabolism | Sterols - metabolism | Ion Channels - metabolism | Humans | Potassium Channels - chemistry | Cell Membrane - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Cholesterol - metabolism | Ion Channel Gating | Ion Channels - chemistry | Index Medicus | Biological Sciences
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5. Full Text Diffracted X-ray tracking method for recording single-molecule protein motions
by Shimizu, Hirofumi
Biochimica et biophysica acta. General subjects, ISSN 0304-4165, 05/2019
Proteins change their conformation depending on function. Although a vast number of static pictures of proteins have been accumulated, information regarding... 
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6. Full Text Long Distance Measurements up to 160 angstrom in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy
by Schmidt, T and Walti, MA and Baber, JL and Hustedt, EJ and Clore, GM
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, ISSN 1433-7851, 12/2016, Volume 55, Issue 51, pp. 15905 - 15909
Current distance measurements between spin-labels on multimeric protonated proteins using double electron-electron resonance (DEER) EPR spectroscopy are... 
PELDOR | KCSA | RELAXATION | MODEL | CHEMISTRY, MULTIDISCIPLINARY | ELDOR | chemical physics | CHANNEL | SOLIDS | ELECTRON-ELECTRON RESONANCE | SPIN-ECHO | spectroscopic methods | structural biology | biophysics | EPR spectroscopy | PULSE EPR
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7. Full Text Selectivity in K⁺ Channels Is Due to Topological Control of the Permeant Ion's Coordinated State
by David L. Bostick and Charles L. Brooks
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2007, Volume 104, Issue 22, pp. 9260 - 9265
The selectivity filter of K⁺ channels provides specific coordinative interactions between dipolar carbonyl ligands, water, and the permeant cation, which allow... 
Molecules | Coordination numbers | Force field | Ligands | Ions | Topology | Modeling | Water channels | Binding sites | Free energy | Solvation structure | Topological constraint | KcsA | Potassium channel | WATER MODEL | MULTIDISCIPLINARY SCIENCES | solvation structure | KCSA POTASSIUM CHANNEL | SIMULATION | HYDRATION | DEPENDENCE | LIGANDS | CHEMISTRY | potassium channel | topological constraint | CHARGE | Potassium Channels - metabolism | Water | Ions - chemistry | Models, Biological | Computer Simulation | Potassium Channels - chemistry | Binding Sites | Index Medicus | Biological Sciences | Physical Sciences
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8. Full Text Ion permeation in K+ channels occurs by direct Coulomb knock-on
by Köpfer, David A and Song, Chen and Gruene, Tim and Sheldrick, George M and Zachariae, Ulrich and De Groot, Bert L
Science, ISSN 0036-8075, 10/2014, Volume 346, Issue 6207, pp. 352 - 355
Potassium channels selectively conduct K+ ions across cellular membranes with extraordinary efficiency. Their selectivity filter exhibits four binding sites... 
INACTIVATION | MOLECULAR-DYNAMICS | MECHANISM | STRUCTURAL BASIS | KCSA | MULTIDISCIPLINARY SCIENCES | RESOLUTION | CONDUCTION | SELECTIVITY FILTER | POTASSIUM CHANNEL | WATER | Potassium - metabolism | Potassium Channels - metabolism | Water | Bacterial Proteins - chemistry | Bacterial Proteins - metabolism | Crystallography, X-Ray | Potassium Channels - chemistry | Protein Conformation | Static Electricity | Binding Sites | Molecular Dynamics Simulation | Potassium | Permeability | Index Medicus | Penetration | Permeation | Selectivity | Channels | Binding sites | Contact | Crystal structure
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9. Full Text Hysteresis of KcsA potassium channel's activation– deactivation gating is caused by structural changes at the channel’s selectivity filter
by Tilegenova, Cholpon and Cortes, D. Marien and Cuello, Luis G
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 03/2017, Volume 114, Issue 12, pp. 3234 - 3239
Hysteresis in hyperpolarization-gated ion channels determines a normal heartbeat, a stable rhythmic firing of pacemaking neurons, and synaptic integration.... 
Biological Sciences | mode-shift | KcsA | C-type inactivation | potassium channels | hysteresis
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10. Full Text Amphipathic antenna of an inward rectifier K⁺ channel responds to changes in the inner membrane leaflet
by Masayuki Iwamoto and Shigetoshi Oiki
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2013, Volume 110, Issue 2, pp. 749 - 754
Membrane lipids modulate the function of membrane proteins. In the case of ion channels, they bias the gating equilibrium, although the underlying mechanism... 
Membrane lipids | Fluorescence | pH | Lipids | Chemical composition | Phospholipids | Potassium channels | Kinetics | P branes | Membrane proteins | Activation gate | Fluorescence measurements | Gating kinetics | pH-dependence | Single-channel current | gating kinetics | ACTIVATION | FULL-LENGTH KCSA | VOLTAGE SENSORS | fluorescence measurements | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | PHOSPHOLIPIDS | KCSA POTASSIUM CHANNEL | activation gate | single-channel current | DEPENDENCE | LIPID-MEMBRANE | PROTEIN FUNCTION | REVEALS | Amino Acid Sequence | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Molecular Sequence Data | Potassium Channels - genetics | Potassium Channels - metabolism | Ion Channel Gating - physiology | Sequence Alignment | Rhodamines | Membrane Lipids - metabolism | Bacterial Proteins - metabolism | Potassium Channels - chemistry | Protein Conformation | Hydrogen-Ion Concentration | Proteins | Membranes | Biochemistry | Potassium | Index Medicus | Biological Sciences
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11. Full Text Investigation of a KcsA Cytoplasmic pH Gate in Lipoprotein Nanodiscs
by Qasim, Arwa and Sher, Inbal and Hirschhorn, Orel and Shaked, Hadassa and Qasem, Zena and Ruthstein, Sharon and Chill, Jordan H
ChemBioChem, ISSN 1439-4227, 03/2019, Volume 20, Issue 6, pp. 813 - 821
The bacterial potassium channel KcsA is gated by pH, opening for conduction under acidic conditions. Molecular determinants responsible for this effect have... 
lipoprotein nanodiscs | NMR spectroscopy | pH gating | KcsA | EPR spectroscopy | ion channels | TETRAMERIZATION | PHOSPHOLIPID-BILAYER NANODISCS | ACTIVATION | CHEMISTRY, MEDICINAL | FULL-LENGTH KCSA | SPIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR DETERMINANTS | PROTEINS | POTASSIUM-CHANNEL | K+ CHANNELS | Nuclear magnetic resonance spectroscopy | Peptides | Hydrogen-ion concentration | Investigations | Conduction | Nuclear magnetic resonance--NMR | Channel gating | Ions | Selectivity | Hydrophobicity | pH effects | Electrostatic properties | Gating | Potassium | Cytoplasm
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12. Full Text Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
by Calcutta, Antonello and Jessen, Christian M and Behrens, Manja Annette and Oliveira, Cristiano L.P and Renart, Maria Lourdes and González-Ros, José M and Otzen, Daniel E and Pedersen, Jan Skov and Malmendal, Anders and Nielsen, Niels Chr
BBA - Biomembranes, ISSN 0005-2736, 09/2012, Volume 1818, Issue 9, pp. 2290 - 2301
Membrane proteins are vital for biological function, and their action is governed by structural properties critically depending on their interactions with the... 
TFE-induced unfolding | Dynamic light scattering | KcsA–surfactant complex | DDM micelle | PCA | Small-angle X-ray scattering | KcsA-surfactant complex | SMALL-ANGLE SCATTERING | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MIXED MICELLES | LATERAL PRESSURE | MASS-SPECTROMETRY | MIXTURES | IN-VITRO | BIOPHYSICS | K+ CHANNEL | BACTERIORHODOPSIN | POTASSIUM CHANNEL KCSA | Escherichia coli - enzymology | Magnetic Resonance Spectroscopy - methods | Models, Chemical | Protein Structure, Secondary | Molecular Conformation | Bacterial Proteins - chemistry | Models, Molecular | Scattering, Small Angle | Protein Folding | Potassium Channels - metabolism | X-Rays | Light | Micelles | Protein Denaturation | Glucosides - chemistry | Bacterial Proteins - metabolism | Potassium Channels - chemistry | Protein Conformation | Scattering, Radiation | Surface-Active Agents - chemistry | Proteins | Surface active agents | Analysis | Methods | Membrane proteins
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13. Full Text Structural mechanism of C-type inactivation in K + channels
by Cortes, D. Marien and Perozo, Eduardo and Cuello, Luis G and Jogini, Vishwanath
Nature, ISSN 0028-0836, 07/2010, Volume 466, Issue 7303, pp. 203 - 208
Interconversion between conductive and non-conductive forms of the K+ channel selectivity filter underlies a variety of gating events, from flicker transitions... 
SHAKER POTASSIUM CHANNELS | KCSA | TETRAETHYLAMMONIUM BLOCKADE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | PORE | SLOW INACTIVATION | MUTATIONS | OPEN STATE | SELECTIVITY FILTER | ION CONDUCTION | Potassium - metabolism | Bacterial Proteins - antagonists & inhibitors | Streptomyces lividans - chemistry | Bacterial Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Structure-Activity Relationship | Potassium Channels - metabolism | Models, Biological | Bacterial Proteins - metabolism | Potassium Channels - chemistry | Protein Conformation | Kinetics | Binding Sites | Ion Channel Gating | Electrons | Ions | Crystal lattices | E coli | Binding sites | Crystal structure | Index Medicus
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14. Full Text Symmetry-constrained analysis of pulsed Double Electron-Electron Resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate
by Dalmas, Olivier and Hyde, H. Clark and Hulse, Raymond E and Perozo, Eduardo
Journal of the American Chemical Society, ISSN 0002-7863, 10/2012, Volume 134, Issue 39, pp. 16360 - 16369
Distance determination from an echo intensity modulation obtained by pulsed double-electron electron resonance (DEER) experiment is a mathematically ill-posed... 
DISTANCE MEASUREMENTS | INACTIVATION | FULL-LENGTH KCSA | CORA | CRYSTAL-STRUCTURE | GATING MECHANISM | ARCHITECTURE | CONFORMATIONAL DYNAMICS | CHEMISTRY, MULTIDISCIPLINARY | POTASSIUM CHANNEL | Potassium Channels - metabolism | Protein Structure, Tertiary | Reproducibility of Results | Protein Multimerization | Bacterial Proteins - chemistry | Protein Structure, Quaternary | Models, Molecular | Streptomyces lividans | Bacterial Proteins - metabolism | Potassium Channels - chemistry | Electron Spin Resonance Spectroscopy - methods | Ion Channel Gating | Measurement | Proteins | Usage | Analysis | Conformational analysis | Electron spectroscopy | Structure | Activation energy | Index Medicus | DEER | distance measurement | spectroscopy | ion channel | KcsA | membrane protein | CorA | pulsed EPR
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15. Full Text Protein interactions central to stabilizing the K⁺ channel selectivity filter in a four-sited configuration for selective K⁺ permeation
by David B. Sauer and Weizhong Zeng and Srinivasan Raghunathan and Youxing Jiang and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2011, Volume 108, Issue 40, pp. 16634 - 16639
The structural and functional conversion of the nonselective NaK channel to a K⁺ selective channel (NaK2K) allows us to identify two key residues. Tyr and Asp... 
Electric potential | Salts | Hydrogen bonds | Molecular structure | Lead | Ions | Potassium channels | Signatures | Potassium | Binding sites | INACTIVATION | ION SELECTIVITY | MECHANISM | KCSA | DETERMINANTS | MULTIDISCIPLINARY SCIENCES | PERSPECTIVES | COORDINATION | NA+ | CONDUCTION | POTASSIUM-CHANNEL | Sodium-Potassium-Exchanging ATPase - metabolism | Sodium-Potassium-Exchanging ATPase - genetics | Electrophysiology | Models, Molecular | Protein Conformation | Crystallography | Amino Acid Motifs | Potassium - chemistry | Proteins | Eukaryotes | Membrane filters | Index Medicus | Biological Sciences
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