F
Francis Rodier
Researcher at Centre national de la recherche scientifique
Publications - 18
Citations - 2500
Francis Rodier is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Seed crystal & Protein Data Bank. The author has an hindex of 13, co-authored 18 publications receiving 2424 citations. Previous affiliations of Francis Rodier include University of Paris-Sud & Stanford University.
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Journal ArticleDOI
The mosaic genome of warm-blooded vertebrates.
Giorgio Bernardi,Birgitta Olofsson,Jan Filipski,Marino Zerial,Julio Salinas,Gérard Cuny,Michele Meunier-Rotival,Francis Rodier +7 more
TL;DR: This approach has revealed that the distribution of genes, integrated viral sequences, and interspersed repeats is highly nonuniform in the genome, and that the base composition and ratio of CpG to GpC in both coding and noncoding sequences, as well as codon usage, mainly depend on the GC content of the isochores harboring the sequences.
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A dissection of specific and non-specific protein-protein interfaces.
TL;DR: A residue propensity score and a hydrophobic interaction score are developed to assess preferences seen in the chemical and amino acid compositions of the different types of interfaces, and indexes are derived to evaluate the atomic packing, which is found to be less compact at non-specific than at specific interfaces.
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Dissecting subunit interfaces in homodimeric proteins.
TL;DR: On average, subunit interfaces in homodimers are twice larger than in complexes, and much less polar due to the large fraction belonging to the core, although the amino acid compositions of the cores are similar in the two types of interfaces.
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Protein-protein interaction at crystal contacts
Joël Janin,Francis Rodier +1 more
TL;DR: Packing contacts are crystal artifacts, yet they make use of the same forces that govern specific recognition in protein‐protein complexes and oligomeric proteins, and provide examples of a nonspecific protein‐ protein interaction which can be compared to biologically relevant ones.
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Hydration of protein–protein interfaces
TL;DR: Water‐mediated polar interactions are as abundant at the interfaces as direct protein–protein hydrogen bonds, and they may contribute to the stability of the assembly.