Marc Guenneugues
Utrecht University
25 Papers
365 Citations
Marc Guenneugues is an academic researcher from Utrecht University. The author has contributed to research in topics: Prokaryotic initiation factor-2 & Rotational diffusion. The author has an hindex of 16, co-authored 25 publications. Previous affiliations of Marc Guenneugues include Centre national de la recherche scientifique.
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Papers
Mapping the fMet‐tRNAfMet binding site of initiation factor IF2
Marc Guenneugues,Enrico Caserta,Letizia Brandi,Roberto Spurio,Sylvie Meunier,Cynthia L. Pon,Rolf Boelens,Claudio O. Gualerzi +7 more
TL;DR: All thermodynamic determinants governing the stability and the specificity of this interaction are localized within the acceptor hexanucleotide fMet‐3′ACCAAC of the initiator tRNA and a fairly small area at the surface of the β‐barrel structure of the 90‐amino acid C‐terminal domain of IF2 (IF2 C‐2).
97
Off-resonance rf fields in heteronuclear NMR: Application to the study of slow motions
TL;DR: In the absence of slow motions the longitudinal and transverse 15N self-relaxation rate values derived are in agreement with the ones measured by the classical inversion-recovery and Carr–Purcell–Meiboom–Gill (CPMG) sequences, respectively.
91
Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails.
Philippe Savarin,Marc Guenneugues,Bernard Gilquin,Hung Lamthanh,Sylvaine Gasparini,Sophie Zinn-Justin,André Ménez +6 more
TL;DR: It is shown that kappa-conotoxin competes with radioactive alpha-dendrotoxin for binding to rat brain synaptosomes, confirming its capacity to bind to potassium channels; however, it behaves as a weak competitor.
90
A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated
TL;DR: A method allowing the determination of the effective B1 field amplitude distribution in a high-resolution NMR spectrometer that essentially consists of a mutation followed by a purging B0 gradient pulse is described.
84
Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus.
Florent Barbault,Céline Landon,Marc Guenneugues,Jean-Philippe Meyer,Valérie Schott,Jean-Luc Dimarcq,Françoise Vovelle +6 more
TL;DR: To the knowledge, Alo-3 is the first peptide from insects with antimicrobial activity adopting the knottin fold, and this finding is validated by the comparison of the structure of Ala-3 with the structures of other structurally related peptides from other sources also showing antifungal activity.