Scan Science and Technology

Contact Leading Edge Experts & Companies

14,000,000 Leading Edge Experts on the ideXlab platform

14,000,000

Leading Edge Experts

on the ideXlab platform

Protein

The Experts below are selected from a list of 12375402 Experts worldwide ranked by ideXlab platform

Protein - Free Register to Access Experts & Abstracts

Reinhard Luhrmann - One of the best experts on this subject based on the ideXlab platform.

  • snrnp sm Proteins share two evolutionarily conserved sequence motifs which are involved in sm Protein Protein interactions
    The EMBO Journal, 1995
    Co-Authors: H Hermann, Veronica A Raker, K Foulaki, H Hornig, H Brahms, Patrizia Fabrizio, Reinhard Luhrmann
    Abstract:

    Abstract The spliceosomal small nuclear ribonucleoProteins (snRNPs) U1, U2, U4/U6 and U5 share eight Proteins B', B, D1, D2, D3, E, F and G which form the structural core of the snRNPs. This class of common Proteins plays an essential role in the biogenesis of the snRNPs. In addition, these Proteins represent the major targets for the so-called anti-Sm auto-antibodies which are diagnostic for systemic lupus erythematosus (SLE). We have characterized the Proteins F and G from HeLa cells by cDNA cloning, and, thus, all human Sm Protein sequences are now available for comparison. Similar to the D, B/B' and E Proteins, the F and G Proteins do not possess any of the known RNA binding motifs, suggesting that other types of RNA-Protein interactions occur in the snRNP core. Strikingly, the eight human Sm Proteins possess mutual homology in two regions, 32 and 14 amino acids long, that we term Sm motifs 1 and 2. The Sm motifs are evolutionarily highly conserved in all of the putative homologues of the human Sm Proteins identified in the data base. These results suggest that the Sm Proteins may have arisen from a single common ancestor. Several hypothetical Proteins, mainly of plant origin, that clearly contain the conserved Sm motifs but exhibit only comparatively low overall homology to one of the human Sm Proteins, were identified in the data base. This suggests that the Sm motifs may also be shared by non-spliceosomal Proteins. Further, we provide experimental evidence that the Sm motifs are involved, at least in part, in Sm Protein-Protein interactions. Specifically, we show by co-immunoprecipitation analyses of in vitro translated B' and D3 that the Sm motifs are essential for complex formation between B' and D3. Our finding that the Sm Proteins share conserved sequence motifs may help to explain the frequent occurrence in patient sera of anti-Sm antibodies that cross-react with multiple Sm Proteins and may ultimately further our understanding of how the snRNPs act as auto-antigens and immunogens in SLE.

Michael Feig - One of the best experts on this subject based on the ideXlab platform.

  • effect of Protein Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
    Physical Chemistry Chemical Physics, 2019
    Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael Feig
    Abstract:

    The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct ProteinProtein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key ProteinProtein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.

  • Effect of ProteinProtein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
    Physical Chemistry Chemical Physics, 2019
    Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael Feig
    Abstract:

    The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct ProteinProtein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key ProteinProtein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.

H Hermann - One of the best experts on this subject based on the ideXlab platform.

  • snrnp sm Proteins share two evolutionarily conserved sequence motifs which are involved in sm Protein Protein interactions
    The EMBO Journal, 1995
    Co-Authors: H Hermann, Veronica A Raker, K Foulaki, H Hornig, H Brahms, Patrizia Fabrizio, Reinhard Luhrmann
    Abstract:

    Abstract The spliceosomal small nuclear ribonucleoProteins (snRNPs) U1, U2, U4/U6 and U5 share eight Proteins B', B, D1, D2, D3, E, F and G which form the structural core of the snRNPs. This class of common Proteins plays an essential role in the biogenesis of the snRNPs. In addition, these Proteins represent the major targets for the so-called anti-Sm auto-antibodies which are diagnostic for systemic lupus erythematosus (SLE). We have characterized the Proteins F and G from HeLa cells by cDNA cloning, and, thus, all human Sm Protein sequences are now available for comparison. Similar to the D, B/B' and E Proteins, the F and G Proteins do not possess any of the known RNA binding motifs, suggesting that other types of RNA-Protein interactions occur in the snRNP core. Strikingly, the eight human Sm Proteins possess mutual homology in two regions, 32 and 14 amino acids long, that we term Sm motifs 1 and 2. The Sm motifs are evolutionarily highly conserved in all of the putative homologues of the human Sm Proteins identified in the data base. These results suggest that the Sm Proteins may have arisen from a single common ancestor. Several hypothetical Proteins, mainly of plant origin, that clearly contain the conserved Sm motifs but exhibit only comparatively low overall homology to one of the human Sm Proteins, were identified in the data base. This suggests that the Sm motifs may also be shared by non-spliceosomal Proteins. Further, we provide experimental evidence that the Sm motifs are involved, at least in part, in Sm Protein-Protein interactions. Specifically, we show by co-immunoprecipitation analyses of in vitro translated B' and D3 that the Sm motifs are essential for complex formation between B' and D3. Our finding that the Sm Proteins share conserved sequence motifs may help to explain the frequent occurrence in patient sera of anti-Sm antibodies that cross-react with multiple Sm Proteins and may ultimately further our understanding of how the snRNPs act as auto-antigens and immunogens in SLE.

Grzegorz Nawrocki - One of the best experts on this subject based on the ideXlab platform.

  • effect of Protein Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
    Physical Chemistry Chemical Physics, 2019
    Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael Feig
    Abstract:

    The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct ProteinProtein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key ProteinProtein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.

  • Effect of ProteinProtein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
    Physical Chemistry Chemical Physics, 2019
    Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael Feig
    Abstract:

    The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct ProteinProtein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key ProteinProtein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.

Angus S Murphy - One of the best experts on this subject based on the ideXlab platform.