Transmembrane channel activity of gramicidin A analogs: Effects of modification and deletion of the amino-terminal residue

1979 ◽  
Vol 132 (4) ◽  
pp. 733-738 ◽  
Author(s):  
J.S. Morrow ◽  
W.R. Veatch ◽  
L. Stryer
Keyword(s):  
Gramicidin A ◽  
Channel Activity ◽  
Terminal Residue ◽  
Amino Terminal ◽  
Transmembrane Channel

scholarly journals Redox-regulated ion channel activity of a cysteine-containing gramicidin A analogue

2006 ◽  
Vol 1758 (4) ◽  
pp. 493-498 ◽  
Author(s):  
Yuri N. Antonenko ◽  
Tatyana B. Stoilova ◽  
Sergey I. Kovalchuk ◽  
Natalya S. Egorova ◽  
Alina A. Pashkovskaya ◽  
...  
Keyword(s):  
Ion Channel ◽  
Gramicidin A ◽  
Channel Activity

Theoretical simulation of ionic transport through a transmembrane channel

1983 ◽  
Vol 61 (8) ◽  
pp. 856-859 ◽  
Author(s):  
Serafin Fraga ◽  
S. H. M. Nilar
Keyword(s):  
Ionic Conduction ◽  
Theoretical Calculations ◽  
Ionic Transport ◽  
Gramicidin A ◽  
Potential Energy Profile ◽  
Theoretical Simulation ◽  
Site Model ◽  
Transmembrane Channel ◽  
Pore Closure ◽  
Terminal Chain

The two-site model of Urry for the ionic conduction through a gramicidin A channel has been confirmed by theoretical calculations, using a method developed at this laboratory, which yields the potential energy profile of the ion along the channel. Preliminary results show that the pore closure could start with the spatial rearrangement of the —HN—CH3 terminal chain under the influence of the ion already in the channel.

GRAMICIDIN A TRANSMEMBRANE CHANNEL: KINETICS OF PACKAGING IN LIPID MEMBRANES

1983 ◽  
pp. 3-10
Author(s):  
LANFRANCO MASOTTI ◽  
PAOLO CAVATORTA ◽  
ALBERTO SPISNI ◽  
EMANUELA CASALI ◽  
GIORGIO SARTOR ◽  
...  
Keyword(s):  
Lipid Membranes ◽  
Gramicidin A ◽  
Channel Kinetics ◽  
Transmembrane Channel ◽  
Kinetics Of

scholarly journals The Gramicidin A Transmembrane Channel: Characteristics of Head-to-Head Dimerized  (L,D) Helices

1971 ◽  
Vol 68 (8) ◽  
pp. 1907-1911 ◽  
Author(s):  
D. W. Urry ◽  
M. C. Goodall ◽  
J. D. Glickson ◽  
D. F. Mayers
Keyword(s):  
Gramicidin A ◽  
Channel Characteristics ◽  
Transmembrane Channel

scholarly journals Structure of the cold- and menthol-sensing ion channel TRPM8

Science ◽  
2017 ◽  
Vol 359 (6372) ◽  
pp. 237-241 ◽  
Author(s):  
Ying Yin ◽  
Mengyu Wu ◽  
Lejla Zubcevic ◽  
William F. Borschel ◽  
Gabriel C. Lander ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Layered Architecture ◽  
Amino Terminal ◽  
Collared Flycatcher ◽  
Transmembrane Channel ◽  
Physiological Processes ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor ◽  
Amino Terminal Domain

Transient receptor potential melastatin (TRPM) cation channels are polymodal sensors that are involved in a variety of physiological processes. Within the TRPM family, member 8 (TRPM8) is the primary cold and menthol sensor in humans. We determined the cryo–electron microscopy structure of the full-length TRPM8 from the collared flycatcher at an overall resolution of ~4.1 ångstroms. Our TRPM8 structure reveals a three-layered architecture. The amino-terminal domain with a fold distinct among known TRP structures, together with the carboxyl-terminal region, forms a large two-layered cytosolic ring that extensively interacts with the transmembrane channel layer. The structure suggests that the menthol-binding site is located within the voltage-sensor–like domain and thus provides a structural glimpse of the design principle of the molecular transducer for cold and menthol sensation.

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