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Showing 1 to 6 of 6 for “"protein disorder"”.

  1. Functional Relevance of Protein Disorder: Why is Disorder Favourable?

    For half a century, the central tenet of protein science has been grounded on the idea that the three-dimensional structure of a protein underlies its function. However, increasing evidence of natively unstructured but functional proteins is accumulating. Termed as intrinsically disordered proteins …

    cambridge Repository record for Functional Relevance of Protein Disorder: Why is Disorder Favourable? (opens in a new tab)

  2. Biophysical mechanisms of intrinsic protein disorder: lessons from a protein backbone model

    Intrinsically disordered regions (IDRs) in proteins populate a dynamic, heterogenous ensemble of structures. Proteins involved in the regulation of critical cellular functions rely on IDRs to carry out their functions. IDRs have been implicated in a number of diseases for which there are currently …

    utmb Repository record for Biophysical mechanisms of intrinsic protein disorder: lessons from a protein backbone model (opens in a new tab)

  3. Mechanisms of binding diversity in protein disorder : molecular recognition features mediating protein interaction networks

    Intrinsically disordered proteins are proteins characterized by lack of stable tertiary structures under physiological conditions. Evidence shows that disordered proteins are not only highly involved in protein interactions, but also have the capability to associate with more than one partner. …

    iupui Repository record for Mechanisms of binding diversity in protein disorder : molecular recognition features mediating protein interaction networks (opens in a new tab)

  4. Probing Order within Intrinsically Disordered Proteins

    Decades have passed since the realisation that a protein’s amino acid sequence can contain all the information required to form a complex three-dimensional fold. Until recently, these encoded structures were thought to be crucial determinants of protein function. Much effort was directed to fully …

    cambridge Repository record for Probing Order within Intrinsically Disordered Proteins (opens in a new tab)

  5. Observing residual structure in disordered peptides with multidimensional infrared spectroscopy

    … 35% of the human proteome is intrinsically disordered. Disordered proteins play a key role in physiologic and pathologic regulation, recognition, and signaling making protein disorder the subject of increasing investigation. Since disordered samples do not generate x-ray quality crystals and …

    mit Repository record for Observing residual structure in disordered peptides with multidimensional infrared spectroscopy (opens in a new tab)

  6. Predicting protein residue-residue contacts and disorder

    … OF MISSOURI AT AUTHOR'S REQUEST.] Predicting a protein's three dimensional structure from its corresponding sequence has long been an extremely important and challenging problem in the field of Structural Bioinformatics. A principle difficulty has been in efficiently exploring the large number …

    missouri Repository record for Predicting protein residue-residue contacts and disorder (opens in a new tab)