Slow Cooperative Folding of a Small Globular Protein HPr (1998)
Robillard, George T., Scheek, Ruud M., Forge, Vincent, Warner, Jessica, Meijberg, Wim, Nuland, Nico A.J. Van, ...
The folding of an 85-residue protein, the histidine-containing phosphocarrier protein HPr, has been studied using a variety of techniques including DSC, CD, ANS fluorescence, and NMR spectroscopy. In...
Detection of residue contacts in a protein folding intermediate
Balbach, Jochen, Forge, Vincent, Lau, Wai Shun, Jones, Jonathan A., Van Nuland, Nico A. J., Dobson, Christopher M.
Protein folding can be described in terms of the development of specific contacts between residues as a highly disordered polypeptide chain converts into the native state. Here we describe an NMR...
Balguerie, Axelle, Dos Reis, Suzana, Ritter, Christiane, Chaignepain, Stéphane, Coulary-Salin, Bénédicte, Forge, Vincent, ...
The [Het-s] infectious element of the fungus Podospora anserina is a prion protein involved in a genetically controlled cell death reaction termed heterokaryon incompatibility. Previous analyses...
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Fändrich, Marcus, Forge, Vincent, Buder, Katrin, Kittler, Marlis, Dobson, Christopher M., Diekmann, Stephan
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure...
Detection of residue contacts in a protein folding intermediate
Balbach, Jochen, Forge, Vincent, Lau, Wai Shun, Jones, Jonathan A., Van Nuland, Nico A. J., Dobson, Christopher M.
Protein folding can be described in terms of the development of specific contacts between residues as a highly disordered polypeptide chain converts into the native state. Here we describe an NMR...
Balguerie, Axelle, Dos Reis, Suzana, Ritter, Christiane, Chaignepain, Stéphane, Coulary-Salin, Bénédicte, Forge, Vincent, ...
The [Het-s] infectious element of the fungus Podospora anserina is a prion protein involved in a genetically controlled cell death reaction termed heterokaryon incompatibility. Previous analyses...
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Fändrich, Marcus, Forge, Vincent, Buder, Katrin, Kittler, Marlis, Dobson, Christopher M., Diekmann, Stephan
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure...
Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
Schanda, Paul, Forge, Vincent, Brutscher, Bernhard
Atom-resolved real-time studies of kinetic processes in proteins have been hampered in the past by the lack of experimental techniques that yield sufficient temporal and atomic resolution. Here we...
Interactions of apomyoglobin with membranes: Mechanisms and effects on heme uptake
Vernier, Grégory, Chenal, Alexandre, Vitrac, Heidi, Barumandzadhe, Roya, Montagner, Caroline, Forge, Vincent
The last step of the folding reaction of myoglobin is the incorporation of a prosthetic group. In cells, myoglobin is soluble, while heme resides in the mitochondrial membrane. We report here an...
Bushmarina, Natalia A., Blanchet, Clément E., Vernier, Grégory, Forge, Vincent
About 30% of proteins require cofactors for their proper folding. The effects of cofactors on the folding reaction have been investigated with α-lactalbumin as a model protein and metal ions as...