Publications associées à Faisceau d'hélices

Opportunities and challenges in design and optimization of protein function

Bruno Emanuel Ferreira De Sousa Correia, Casper Alexander Goverde

The field of protein design has made remarkable progress over the past decade. Historically, the low reliability of purely structure-based design methods limited their application, but recent strategies that combine structure-based and sequence-based calcu ...

Nature Portfolio2024

Microsecond Time-Resolved Cryo-Electron Microscopy

Oliver Florian Harder

Recently, single-particle cryo-electron microscopy emerged as a technique capable of determining protein structures at near-atomic resolution and resolving protein dynamics with a temporal resolution ranging from second to milliseconds. This thesis describ ...

EPFL2024

Fast viral dynamics revealed by microsecond time-resolved cryo-EM

Marcel Drabbels, Ulrich Lorenz, Sarah Victoria Barrass, Oliver Florian Harder

Observing proteins as they perform their tasks has largely remained elusive, which has left our understanding of protein function fundamentally incom- plete. To enable such observations, we have recently proposed a technique that improves the time resoluti ...

Nature Research2023

Unintended specificity of an engineered ligand-binding protein facilitated by unpredicted plasticity of the protein fold

Kai Johnsson, Alberto Schena

Attempts to create novel ligand-binding proteins often focus on formation of a binding pocket with shape complementarity against the desired ligand (particularly for compounds that lack distinct polar moieties). Although designed proteins often exhibit bin ...

OXFORD UNIV PRESS2018

Phage selection of chemically stabilized alpha-helical peptide ligands

Christian Heinis, Jörg Hülsken, Pierre Vincent Dessen, Philippe Diderich, Davide Bertoldo, Maola Khan Mohammad Golam

Short alpha-helical peptides stabilized by linkages between constituent amino acids offer an attractive format for ligand development. In recent years, a range of excellent ligands based on stabilized alpha-helices were generated by rational design using a ...

2016

Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4

Laure Menin, Petr Leiman, Sergii Buth

Gene product 5 (gp5) of bacteriophage T4 is a spike-shaped protein that functions to disrupt the membrane of the target cell during phage infection. Its C-terminal domain is a long and slender -helix that is formed by three polypeptide chains wrapped aroun ...

Mdpi Ag2015

Development of bicyclic peptide Her2 binders and phage selection of alpha-helical peptide ligands

Philippe Diderich

Conformationally constrained peptide ligands offer an attractive format for the development of therapeutics. They can bind with high affinity and selectivity to protein targets, they are small enough to diffuse into tissues, they can be synthesized chemica ...

EPFL2014

Mechanism to Trigger Unfolding in O6--Alkylguanine-DNA Alkyltransferase

Ursula Röthlisberger, Elizabeth Claire Brunk, Birgit Mollwitz

O6-alkylguanine-DNA alkyltransferase (AGT) adopts a non-enzymatic suicide mechanism for the repair of methylated guanine bases by transferring the methyl adduct to itself, thereby initiating unfolding and fast degradation. Classical molecular dynamics simu ...

Wiley-Blackwell2013

Time Scales of Slow Motions in Ubiquitin Explored by Heteronuclear Double Resonance

Geoffrey Bodenhausen, Simone Ulzega, Nicola Salvi, Fabien Ferrage

Understanding how proteins function at the atomic level relies in part on a detailed characterization of their dynamics. Ubiquitin, a small single-domain protein, displays rich dynamic properties over a wide range of time scales. In particular, several reg ...

2012

A nonradial coarse-grained potential for proteins produces naturally stable secondary structure elements

Matteo Dal Peraro, Michele Cascella, Davide Alemani, Francesca Collu

We introduce a nonradial potential term for coarse-grained (CG) molecular simulations of proteins. This term mimics the backbone dipole−dipole interactions and accounts for the needed directionality to form stable folded secondary structure elements. We sh ...

2010

PEG-based hybrid block copolymers containing α-helical coiled coil peptide sequences: Control of self-assembly and preliminary biological evaluation

Harm-Anton Klok

This study investigates the structure and organization of a series of hybrid diblock copolymers based on polyethylene glycol) (PEG) and peptide sequences inspired by the coiled coil protein folding motif. Circular dichroism spectroscopy and analytical ultr ...

American Chemical Society2005