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Showing 1 to 5 of 5 for “"Folded domains"”.

  1. UNIQUE ALLOSTERIC MECHANISM REGULATING PROTEIN-PROTEIN INTERACTION THROUGH PHOSPHORYLATION: A CASE STUDY OF THE CONFORMATIONAL CHANGES IN THE SYK TANDEM SH2 PROTEIN

    … Syk is a 72-kDa kinase comprising three folded domains: two SH2 domains and a catalytic domain. The tandem SH2 domains connected by linker A are key to the regulation of Syk activity. Immune signaling through Syk is initiated by the binding of the tandem SH2 to the dpITAMs found on immune …

    purdue-thes Repository record for UNIQUE ALLOSTERIC MECHANISM REGULATING PROTEIN-PROTEIN INTERACTION THROUGH PHOSPHORYLATION: A CASE STUDY OF THE CONFORMATIONAL CHANGES IN THE SYK TANDEM SH2 PROTEIN (opens in a new tab)

  2. Mechanics of the hysteretic large strain behavior of mussel byssus threads

    … banana-shaped filament bundles, with molecular folded domain ends. It is demonstrated that as the thread is stretched these bundles straighten and the ends unfold, increasing the tension-free length of the filaments. Further stretching is required to load this new length and to release more of …

    mit Repository record for Mechanics of the hysteretic large strain behavior of mussel byssus threads (opens in a new tab)

  3. Delineating the Mechanisms of Misfolded Endoplasmic Reticulum (ER) Luminal Protein Retrotranslocation for ER-Associated Degradation

    … roles elucidated, it remains less clear how folded domains on ERAD clients complicate their extraction from the ER and degradation. To address this, we used several luminal ERAD substrates with well-defined structural properties. Deglycosylation and digitonin permeabilization assays were used …

    tenn-hsc Repository record for Delineating the Mechanisms of Misfolded Endoplasmic Reticulum (ER) Luminal Protein Retrotranslocation for ER-Associated Degradation (opens in a new tab)

  4. Characterizing Multivalent Interactions Between Folded Protein Domains and Intrinsically Disordered Regions or Peptide Substrates

    … with a focus on interactions between structured domains and intrinsically disordered regions or peptide substrates.The subject of Chapter two is prolyl isomerase Ess1, which is an essential enzyme found in Saccharomyces cerevisiae. Ess1 regulates the transcription and co-transcriptional RNA …

    syracuse-diss Repository record for Characterizing Multivalent Interactions Between Folded Protein Domains and Intrinsically Disordered Regions or Peptide Substrates (opens in a new tab)

  5. Force-dependent changes in alpha-catenin conformation

    … a mutation designed to mimic this partially unfolded conformation resulted in exposure of a buried residue in the putative actin-binding site. These results suggest that tension-dependent conformational changes allosterically regulate actin binding by promoting a high-affinity conformation of …

    uiuc Repository record for Force-dependent changes in alpha-catenin conformation (opens in a new tab)