Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations

ACS Nano ◽  
2020 ◽  
Author(s):  
David P. Hoogerheide ◽  
Tatiana K. Rostovtseva ◽  
Daniel Jacobs ◽  
Philip A. Gurnev ◽  
Sergey M. Bezrukov
Keyword(s):  
Membrane Protein ◽  
Protein Binding ◽  
Peripheral Membrane Protein

scholarly journals Ultra-Sensitive Detection of Peripheral Membrane Protein Binding to the Plasma Membrane of Living Cells

2019 ◽  
Vol 116 (3) ◽  
pp. 283a
Author(s):  
Isaac Angert ◽  
John Kohler ◽  
Siddarth Reddy Karuka ◽  
Morgan E. Meissner ◽  
Louis M. Mansky ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Protein Binding ◽  
Living Cells ◽  
Sensitive Detection ◽  
Peripheral Membrane Protein

scholarly journals A Role for Weak Electrostatic Interactions in Peripheral Membrane Protein Binding

2016 ◽  
Vol 110 (6) ◽  
pp. 1367-1378 ◽  
Author(s):  
Hanif M. Khan ◽  
Tao He ◽  
Edvin Fuglebakk ◽  
Cédric Grauffel ◽  
Boqian Yang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Binding ◽  
Electrostatic Interactions ◽  
Peripheral Membrane Protein

scholarly journals Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering—A Comparison between Wild-Type Protein and a Hinge Mutant

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0128954 ◽  
Author(s):  
Saara Laulumaa ◽  
Tuomo Nieminen ◽  
Mari Lehtimäki ◽  
Shweta Aggarwal ◽  
Mikael Simons ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neutron Scattering ◽  
Wild Type ◽  
Type Protein ◽  
Wild Type Protein ◽  
Peripheral Membrane Protein

scholarly journals The structure of a tail‐anchor membrane protein‐binding complex reveals the regulation of Get3 by Get4 (950.4)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Harry Gristick ◽  
Meera Rao ◽  
Justin Chartron ◽  
Mike Rome ◽  
Shu‐ou Shan ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Binding

scholarly journals Novel 45-Kilodalton Leptospiral Protein That Is Processed to a 31-Kilodalton Growth-Phase-Regulated Peripheral Membrane Protein

2002 ◽  
Vol 70 (1) ◽  
pp. 323-334 ◽  
Author(s):  
James Matsunaga ◽  
Tracy A. Young ◽  
Jeanne K. Barnett ◽  
Dean Barnett ◽  
Carole A. Bolin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Peptide Mapping ◽  
Immunoblot Analysis ◽  
Mammalian Host ◽  
Protein Antigens ◽  
Expression Library ◽  
Genomic Expression ◽  
Amino Terminal ◽  
Peripheral Membrane Protein ◽  
Low Passage

ABSTRACT Leptospiral protein antigens are of interest as potential virulence factors and as candidate serodiagnostic and immunoprotective reagents. We identified leptospiral protein antigens by screening a genomic expression library with serum from a rabbit hyperimmunized with formalin-killed, virulent Leptospira kirschneri serovar grippotyphosa. Genes expressing known outer membrane lipoproteins LipL32 and LipL41, the heat shock protein GroEL, and the α, β, and β′ subunits of RNA polymerase were isolated from the library. In addition, a new leptospiral gene that in Escherichia coli expressed a 45-kDa antigen with an amino-terminal signal peptide followed by the spirochetal lipobox Val−4-Phe−3-Asn−2-Ala−1↓Cys+1 was isolated. We designated this putative lipoprotein LipL45. Immunoblot analysis of a panel of Leptospira strains probed with LipL45 antiserum demonstrated that many low-passage strains expressed LipL45. In contrast, LipL45 was not detected in high-passage, culture-attenuated strains, suggesting that LipL45 is a virulence-associated protein. In addition, all leptospiral strains tested, irrespective of culture passage, expressed a 31-kDa antigen that was recognized by LipL45 antiserum. Southern blot and peptide mapping studies indicated that this 31-kDa antigen was derived from the carboxy terminus of LipL45; therefore, it was designated P31LipL45. Membrane fractionation studies demonstrated that P31LipL45 is a peripheral membrane protein. Finally, we found that P31LipL45 levels increased as Leptospira entered the stationary phase, indicating that P31LipL45 levels were regulated. Hamsters infected with L. kirschneri formed an antibody response to LipL45, indicating that LipL45 was expressed during infection. Furthermore, the immunohistochemistry of kidneys from infected hamsters indicated that LipL45 was expressed by L. kirschneri that colonized the renal tubule. These observations suggest that expression of LipL45 responds to environmental cues, including those encountered during infection of a mammalian host.

Influence of the physicochemical environment on membrane-protein binding: investigation using a fabricated PVDF membrane

2015 ◽  
Vol 35 (4) ◽  
pp. 339-347
Author(s):  
Abdul L. Ahmad ◽  
Norhidayah Ideris ◽  
Ooi Boon Seng ◽  
Low Siew Chun ◽  
Asma Ismail
Keyword(s):  
Membrane Protein ◽  
Protein Binding ◽  
Polyvinylidene Fluoride ◽  
Pvdf Membrane ◽  
Ph Values ◽  
Symmetric Structure ◽  
Binding Mechanisms

Abstract The correlation between the behavior of a polyvinylidene fluoride (PVDF) membrane toward protein binding at different physicochemical environments was investigated. The PVDF membrane was first fabricated and characterized to understand its morphological, polymorph and intrinsic characteristics. The results confirmed that the membrane had a microporous, symmetric structure and high hydrophobicity and electronegativity. The membrane was further tested under different physicochemical environments by modifying the type of protein and pH medium used. The results showed that different proteins and pH values contribute to different membrane-protein binding mechanisms. Overall, the results of PVDF membrane-protein binding were satisfactory and demonstrated the ability of the membrane to capture various proteins or reagents.

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