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 …

[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 …

Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37

KA Henzler Wildman, DK Lee, A Ramamoorthy - Biochemistry, 2003 - ACS Publications
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 …

MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain

KJ Hallock, DK Lee, A Ramamoorthy - Biophysical journal, 2003 - cell.com
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 …

Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket

EN Schmidt, D Lamprinaki, KA McCord, M Joe… - Nature …, 2023 - nature.com
Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands.
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 …

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

G Harauz, N Ishiyama, CMD Hill, IR Bates, DS Libich… - Micron, 2004 - Elsevier
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 …

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 …

Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin

A Ramamoorthy, S Thennarasu, DK Lee, A Tan… - Biophysical journal, 2006 - cell.com
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 …

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 …