Publication
Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide
Publications associées (37)
Solution nuclear magnetic resonance spectroscopy of bacterial outer membrane proteins in natively excreted vesicles using engineered Escherichia coli
Gaining structural information on membrane proteins in their native lipid environment is a long-standing challenge in molecular biology. Instead, it is common to employ membrane mimetics, which has been shown to affect protein structure, dynamics, and func ...
WILEY2022Towards automating de novo protein design for novel functionalities: controlling protein folds and protein-protein interactions
The sheer size of the protein sequence space is massive: a protein of 100 residues can have 20^100 possible sequence combinations; and knowing that this exceeds the number of atoms in the universe, the chance of randomly discovering a stable new sequence w ...
EPFL2022Similarities and Differences among Protein Dynamics Studied by Variable Temperature Nuclear Magnetic Resonance Relaxation
David Lyndon Emsley, Jayasubba Reddy Yarava, Andrea Bertarello, Baptiste Busi, François Freymond
Understanding and describing the dynamics of proteins is one of the major challenges in biology. Here, we use multifield variable-temperature NMR longitudinal relaxation (R-1) measurements to determine the hierarchical activation energies of motions of fou ...
AMER CHEMICAL SOC2021Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization
Matteo Dal Peraro, Luciano Andres Abriata
Continuous assessment of transferable forcefields for molecular simulations is essential to identify their weaknesses and direct improvement efforts. The latest efforts focused on better describing disordered proteins while retaining proper description of ...
2021Crosslinking Allosteric Sites on the Nucleosome Core Particle
Designing compounds that bind to the acidic patch of the nucleosome core particle (NCP) is an emerging therapeutic approach that can inhibit the binding of key chromatin factors. Pretreatment of human ovarian carcinoma, A2780, cells with RAPTA-T, an antime ...
EPFL2019Structural and functional analysis of host attachment proteins from contractile injection systems
Bacteriophages of the myoviridae family, R-type pyocin, Photorhabus virulence cassette (PVC), Serratia antifeeding prophage (Afp) and type 6 secretion system (T6SS) form a class of contractile injection systems that share common structural and functional c ...
EPFL2018Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins
Paolo De Los Rios, Alessandro Barducci, Pierre Goloubinoff, Bruno Claude Daniel Fauvet, Alberto Stefano Sassi
Protein homeostasis, namely the ensemble of cellular mechanisms collectively controlling the activity, stability and conformational states of proteins, depends on energy-consuming processes. De novo protein synthesis requires ATP hydrolysis for peptide bon ...
2017Polar Hinges as Functionalized Conformational Constraints in (Bi) cyclic Peptides
Christian Heinis, Sangram Shivdas Kale
Two polar hinges for cyclization of peptides have been developed, leading to bicyclic peptides and cyclized peptides with improved solubility and biological activity. Increasingly, we note that a good aqueous solubility of peptides is an absolute prerequis ...
Wiley-Blackwell2017Middle-down approaches for mass spectrometry-based protein identification and characterization
Mass spectrometry (MS) has emerged over the last two decades as the analytical technique of choice in systems-level protein studies, known as proteomics. Two are the MS-based approaches generally applied to proteomics: bottom-up (BU), which relies on the p ...
EPFL2016Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding
Matteo Dal Peraro, Luciano Andres Abriata
Protein-protein recognition and binding are governed by diffusion, noncovalent forces and conformational flexibility, entangled in a way that only molecular dynamics simulations can dissect at high resolution. Here we exploited ubiquitin's noncovalent dime ...
Nature Publishing Group2015