• Publications
  • Influence
Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46
The nuclear magnetic resonance (NMR) solution structure of acidocin B in sodium dodecyl sulfate micelles was elucidated, revealing that it is composed of four α-helices of similar length that are folded to form a compact, globular bundle with a central pore. Expand
Nuclear Magnetic Resonance Solution Structures of Lacticin Q and Aureocin A53 Reveal a Structural Motif Conserved among Leaderless Bacteriocins with Broad-Spectrum Activity.
In inhibition studies, inhibition studies showed that LnqQ and AucA have different antimicrobial potency against the Gram-positive strains tested, suggesting that sequence disparities play a crucial role in their mechanisms of action. Expand
Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide.
The first three-dimensional structures of enterocins 7A and 7B, leaderless bacteriocins recently isolated from Enterococcus faecalis 710C are reported, showing an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold. Expand
NMR Conformational Analyses on (des-bromo) Neuropeptide B [1–23] and Neuropeptide W [1–23]: The Importance of α-helices, a Cation-π Interaction and a β-Turn
Abstract The preferred conformations of the orphan G-protein coupled receptor agonists (des-bromo) neuropeptide B [1–23] and neuropeptide W [1–23], referred to as NPB and NPW, have been determined byExpand
NMR conformational analyses on (des-bromo) neuropeptide B [1-23] and neuropeptide W [1-23]: the importance of alpha-helices, a cation-pi interaction and a beta-turn.
The preferred conformations of the orphan G-protein coupled receptor agonists (des-bromo) neuropeptide B and NPW are determined by (1)H NMR, CD, and molecular modeling and it is postulated that the N-terminus is involved in membrane recognition and receptor binding. Expand
Solution Structures of Phenol-Soluble Modulins α1, α3, and β2, Virulence Factors from Staphylococcus aureus.
Three of these peptide toxins, PSMs α1, α3, and β2, normally produced by Staphylococcus aureus, have been synthesized using solid-supported peptide synthesis (SPPS) or made by heterologous expression in Escherichia coli (PSMβ2). Expand
Identification and three‐dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria
It is reported that CbnX and CbnY comprise a class IIb (two‐component) bacteriocin in Carnobacteria and does not appear to interact directly and likely require a membrane‐bound receptor to facilitate formation of the bacteriOCin complex. Expand
A ruthenium-dihydrogen putative intermediate in ketone hydrogenation.
A 1H NMR study concludes that the dihydrogen ligand in 2' does not protonate 2-PrOH to a catalytically significant extent, and that 2' requires an added base or hydride source to be an active catalyst. Expand