The magic of bicelles lights up membrane protein structure
UHN Dürr, M Gildenberg, A Ramamoorthy - Chemical reviews, 2012 - ACS Publications
Biological membranes and membrane proteins, responsible for numerous exciting
biological processes, present one of the paramount challenges in biophysics today …
biological processes, present one of the paramount challenges in biophysics today …
[HTML][HTML] The human beta-defensin-3, an antibacterial peptide with multiple biological functions
V Dhople, A Krukemeyer, A Ramamoorthy - Biochimica et Biophysica Acta …, 2006 - Elsevier
A group of interesting molecules called defensins exhibit multiple functions but have been
primarily recognized to possess a broad spectrum of antimicrobial activities. Studies have …
primarily recognized to possess a broad spectrum of antimicrobial activities. Studies have …
Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
LL-37 is an amphipathic, α-helical, antimicrobial peptide. 15N chemical shift and 15N
dipolar− shift spectroscopy of site-specifically labeled LL-37 in oriented lipid bilayers …
dipolar− shift spectroscopy of site-specifically labeled LL-37 in oriented lipid bilayers …
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
In this work, we present the first characterization of the cell lysing mechanism of MSI-78, an
antimicrobial peptide. MSI-78 is an amphipathic α-helical peptide designed by Genaera …
antimicrobial peptide. MSI-78 is an amphipathic α-helical peptide designed by Genaera …
Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket
Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands.
Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing …
Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing …
[HTML][HTML] Impact of membrane curvature on amyloid aggregation
MS Terakawa, Y Lin, M Kinoshita, S Kanemura… - … et Biophysica Acta (BBA …, 2018 - Elsevier
The misfolding, amyloid aggregation, and fibril formation of intrinsically disordered
proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders …
proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders …
Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin
sheath in the central nervous system of higher vertebrates, and a member of a larger family …
sheath in the central nervous system of higher vertebrates, and a member of a larger family …
Chemical shift tensor–The heart of NMR: Insights into biological aspects of proteins
H Saitô, I Ando, A Ramamoorthy - Progress in nuclear magnetic resonance …, 2010 - Elsevier
The chemical shift of a nucleus, i, in a molecule arises from the nuclear shielding effect of an
applied magnetic field, caused by an induced magnetic field resulting from circulation of …
applied magnetic field, caused by an induced magnetic field resulting from circulation of …
Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
The mechanism of membrane interaction of two amphipathic antimicrobial peptides, MSI-78
and MSI-594, derived from magainin-2 and melittin, is presented. Both the peptides show …
and MSI-594, derived from magainin-2 and melittin, is presented. Both the peptides show …
Direct observation of lipid bilayer disruption by poly (amidoamine) dendrimers
A Mecke, S Uppuluri, TM Sassanella, DK Lee… - Chemistry and physics …, 2004 - Elsevier
Atomic force microscopy (AFM) is employed to observe the effect of poly
(amidoamine)(PAMAM) dendrimers on 1, 2-dimyristoyl-sn-glycero-3-phosphocholine …
(amidoamine)(PAMAM) dendrimers on 1, 2-dimyristoyl-sn-glycero-3-phosphocholine …