Voltage Gating Interactions of the Protein Lysenin with Metal Ions in an Artificial Lipid Bilayer

Tyler Clark; Sheenah Bryant; Steve Rossland; Eric Krueger; Charles Hanna; Daniel Fologea

Voltage Gating Interactions of the Protein Lysenin with Metal Ions in an Artificial Lipid Bilayer

Tyler Clark, Sheenah Bryant, Steve Rossland, Eric Krueger, Charles Hanna, Daniel Fologea

Physics Department

Boise State University

Research output: Contribution to conference › Poster

Abstract

Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lysenin. These channels are voltage regulated and are responsive to changes in metal ion concentration. In our research, we studied the effects of metal ion concentration on the lysenin channel’s voltage regulated gating, using both multivalent and monovalent metals. A model was developed to explain the apparent subunit cooperativity within the lysenin channel. The model allows for the complex reaction to changing concentration of metal ions, and offers knowledge of the lysenin channel’s internal workings.

Original language	American English
State	Published - 21 Apr 2014
Event	Undergraduate Research and Scholarship Conference 2014 - Boise State University, Boise, United States Duration: 21 Apr 2014 → 21 Apr 2014 https://scholarworks.boisestate.edu/2014_under_conf

Conference

Conference	Undergraduate Research and Scholarship Conference 2014
Abbreviated title	URS 2014
Country/Territory	United States
City	Boise
Period	21/04/14 → 21/04/14
Internet address	https://scholarworks.boisestate.edu/2014_under_conf

Keywords

lysenin

EGS Disciplines

Biological and Chemical Physics

Access to Document

https://scholarworks.boisestate.edu/as_14/59/

Cite this

@conference{566ab6ce03a6453197728a98378ca511,

title = "Voltage Gating Interactions of the Protein Lysenin with Metal Ions in an Artificial Lipid Bilayer",

abstract = "Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lysenin. These channels are voltage regulated and are responsive to changes in metal ion concentration. In our research, we studied the effects of metal ion concentration on the lysenin channel{\textquoteright}s voltage regulated gating, using both multivalent and monovalent metals. A model was developed to explain the apparent subunit cooperativity within the lysenin channel. The model allows for the complex reaction to changing concentration of metal ions, and offers knowledge of the lysenin channel{\textquoteright}s internal workings.",

keywords = "lysenin",

author = "Tyler Clark and Sheenah Bryant and Steve Rossland and Eric Krueger and Charles Hanna and Daniel Fologea",

year = "2014",

month = apr,

day = "21",

language = "American English",

note = "Undergraduate Research and Scholarship Conference 2014, URS 2014 ; Conference date: 21-04-2014 Through 21-04-2014",

url = "https://scholarworks.boisestate.edu/2014\_under\_conf",

}

TY - CONF

T1 - Voltage Gating Interactions of the Protein Lysenin with Metal Ions in an Artificial Lipid Bilayer

AU - Clark, Tyler

AU - Bryant, Sheenah

AU - Rossland, Steve

AU - Krueger, Eric

AU - Hanna, Charles

AU - Fologea, Daniel

PY - 2014/4/21

Y1 - 2014/4/21

N2 - Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lysenin. These channels are voltage regulated and are responsive to changes in metal ion concentration. In our research, we studied the effects of metal ion concentration on the lysenin channel’s voltage regulated gating, using both multivalent and monovalent metals. A model was developed to explain the apparent subunit cooperativity within the lysenin channel. The model allows for the complex reaction to changing concentration of metal ions, and offers knowledge of the lysenin channel’s internal workings.

AB - Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lysenin. These channels are voltage regulated and are responsive to changes in metal ion concentration. In our research, we studied the effects of metal ion concentration on the lysenin channel’s voltage regulated gating, using both multivalent and monovalent metals. A model was developed to explain the apparent subunit cooperativity within the lysenin channel. The model allows for the complex reaction to changing concentration of metal ions, and offers knowledge of the lysenin channel’s internal workings.

KW - lysenin

M3 - Poster

T2 - Undergraduate Research and Scholarship Conference 2014

Y2 - 21 April 2014 through 21 April 2014

ER -

Voltage Gating Interactions of the Protein Lysenin with Metal Ions in an Artificial Lipid Bilayer

Abstract

Conference

Keywords

EGS Disciplines

Access to Document

Fingerprint

Cite this