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Showing 1 to 5 of 5 for “"Protein Structure, Tertiary"”.

  1. Studies on Combining Sequence and Structure for Protein Classification

    … is to develop a better understanding of how proteins evolve different structures and functions. A large scale protein clustering can provide a useful platform to identify such principles of protein evolution. Manual classification schemes accurately group homologous proteins, but they are …

    utswmed Repository record for Studies on Combining Sequence and Structure for Protein Classification (opens in a new tab)

  2. Structural Analysis of Domain Swapping in the Protein Kinase: Crystal Structure of Human Ste20 OSR1 Kinase Domain

    Ste20p (Sterile 20 protein) is a yeast MAP4K involved in the pheromoneresponsive MAPK cascade of the mating pathway. Recent studies reveal that its homologs in mammals, Drosophila melanogaster, Caenorhabditis elegans and other organisms constitute a large emerging group of protein kinases including …

    utswmed Repository record for Structural Analysis of Domain Swapping in the Protein Kinase: Crystal Structure of Human Ste20 OSR1 Kinase Domain (opens in a new tab)

  3. Regulation of Endocytosis of ROMK Channel by WNK Kinase Family

    … (ITSN) is a multimodular endocytic scaffold protein. The proline-rich domains of WNK1 and WNK4 bind with the Src-homology domain (SH3) of intersectin, and this interaction is important for the stimulation of endocytosis of ROMK by WNKs. Intersectin will further activate the GTPase activity of …

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  4. Chemical Footprinting of Polymeric Structure of hnRNPA2 Low Complexity Domain

    Many DNA and RNA regulatory proteins contain polypeptide domains that are unstructured when analyzed in cell lysates. These domains are typified by an over-representation of a limited number of amino acids and have been termed prion-like, intrinsically disordered or low complexity domains. These …

    utswmed Repository record for Chemical Footprinting of Polymeric Structure of hnRNPA2 Low Complexity Domain (opens in a new tab)

  5. HAMP Domain and Signaling Mechanism of the Aer Protein

    <p><em>Escherichia coli</em> utilizes the Aer protein to sense changes in the intracellular energy level and guide the bacteria to a niche where the cellular energy level is optimal. Aer contains a PAS sensory domain and an FI fragment in the N terminus and a chemotaxis signaling domain in the C …

    loma-linda Repository record for HAMP Domain and Signaling Mechanism of the Aer Protein (opens in a new tab)