scholarly journals ‘Shooting gallery’ for membrane proteins provides new insights into complexities of their function and structural dynamics

2015 ◽  
Vol 593 (2) ◽  
pp. 353-354 ◽  
Author(s):  
Boris Martinac ◽  
Jamie Vandenberg
Keyword(s):  
Membrane Proteins ◽  
Structural Dynamics ◽  
Shooting Gallery

scholarly journals Structural dynamics of membrane proteins

2017 ◽  
Vol 73 (a2) ◽  
pp. C100-C100
Author(s):  
So Iwata
Keyword(s):  
Membrane Proteins ◽  
Structural Dynamics

scholarly journals The Role of a Crystallographically Unresolved Cytoplasmic Loop in Stabilizing the Bacterial Membrane Insertase YidC2

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Thomas Harkey ◽  
Vivek Govind Kumar ◽  
Jeevapani Hettige ◽  
Seyed Hamid Tabari ◽  
Kalyan Immadisetty ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structural Dynamics ◽  
Md Simulations ◽  
Protein Assembly ◽  
Bacillus Halodurans ◽  
Bacterial Membrane ◽  
Apparent Lack ◽  
Head Groups ◽  
Cytoplasmic Loops

Abstract YidC, a bacterial member of the YidC/Alb3/Oxa1 insertase family, mediates membrane protein assembly and insertion. Cytoplasmic loops are known to have functional significance in membrane proteins such as YidC. Employing microsecond-level molecular dynamics (MD) simulations, we show that the crystallographically unresolved C2 loop plays a crucial role in the structural dynamics of Bacillus halodurans YidC2. We have modeled the C2 loop and used all- atom MD simulations to investigate the structural dynamics of YidC2 in its apo form, both with and without the C2 loop. The C2 loop was found to stabilize the entire protein and particularly the C1 region. C2 was also found to stabilize the alpha-helical character of the C-terminal region. Interestingly, the highly polar or charged lipid head groups of the simulated membranes were found to interact with and stabilize the C2 loop. These findings demonstrate that the crystallographically unresolved loops of membrane proteins could be important for the stabilization of the protein despite the apparent lack of structure, which could be due to the absence of the relevant lipids to stabilize them in crystallographic conditions.

scholarly journals Using Click Chemistry and Voltage Clamp Fluorimetry to Study Structural Dynamics of Membrane Proteins

2019 ◽  
Vol 116 (3) ◽  
pp. 542a
Author(s):  
Kanchan Gupta ◽  
Gilman E.S. Toombes ◽  
Kenton J. Swartz
Keyword(s):  
Membrane Proteins ◽  
Click Chemistry ◽  
Voltage Clamp ◽  
Structural Dynamics

scholarly journals Single-molecule fret study on structural dynamics of membrane proteins

2020 ◽  
Author(s):  
◽  
Atieh Aminian Jazi
Keyword(s):  
Membrane Proteins ◽  
Structural Dynamics ◽  
Single Molecule ◽  
Single Molecule Fret

scholarly journals The Role of a Crystallographically Unresolved Cytoplasmic Loop in Stabilizing the Bacterial Membrane Insertase YidC2

2019 ◽  
Author(s):  
Thomas Harkey ◽  
Vivek Govind Kumar ◽  
Jeevapani Hettige ◽  
Seyed Hamid Tabari ◽  
Kalyan Immadisetty ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structural Dynamics ◽  
Md Simulations ◽  
Protein Assembly ◽  
Bacillus Halodurans ◽  
Bacterial Membrane ◽  
Apparent Lack ◽  
Head Groups ◽  
Cytoplasmic Loops

ABSTRACTYidC, a bacterial member of the YidC/Alb3/Oxa1 insertase family, mediates membrane protein assembly and insertion. Cytoplasmic loops are known to have functional significance in membrane proteins such as YidC. Employing microsecond-level molecular dynamics (MD) simulations, we show that the crystallographically unresolved C2 loop plays a crucial role in the structural dynamics of Bacillus halodurans YidC2. We have modeled the C2 loop and used allatom MD simulations to investigate the structural dynamics of YidC2 in its apo form, both with and without the C2 loop. The C2 loop was found to stabilize the entire protein and particularly the C1 region. C2 was also found to stabilize the alpha-helical character of the C-terminal region. Interestingly, the highly polar or charged lipid head groups of the simulated membranes were found to interact with and stabilize the C2 loop. These findings demonstrate that the crystallographically unresolved loops of membrane proteins could be important for the stabilization of the protein despite the apparent lack of structure, which could be due to the absence of the relevant lipids to stabilize them in crystallographic conditions.

scholarly journals Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques

Biophysica ◽  
2021 ◽  
Vol 1 (2) ◽  
pp. 106-125
Author(s):  
Indra D. Sahu ◽  
Gary A. Lorigan
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Membrane Proteins ◽  
Structural Dynamics ◽  
Conformational Dynamics ◽  
Biological Significance ◽  
Spectroscopic Techniques ◽  
Paramagnetic Resonance ◽  
Site Directed Spin Labeling ◽  
Living Organisms ◽  
Electron Paramagnetic

Membrane proteins are essential for the survival of living organisms. They are involved in important biological functions including transportation of ions and molecules across the cell membrane and triggering the signaling pathways. They are targets of more than half of the modern medical drugs. Despite their biological significance, information about the structural dynamics of membrane proteins is lagging when compared to that of globular proteins. The major challenges with these systems are low expression yields and lack of appropriate solubilizing medium required for biophysical techniques. Electron paramagnetic resonance (EPR) spectroscopy coupled with site directed spin labeling (SDSL) is a rapidly growing powerful biophysical technique that can be used to obtain pertinent structural and dynamic information on membrane proteins. In this brief review, we will focus on the overview of the widely used EPR approaches and their emerging applications to answer structural and conformational dynamics related questions on important membrane protein systems.

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