Sökning: "unfolded protein"

Visar resultat 1 - 5 av 86 avhandlingar innehållade orden unfolded protein.

  1. 1. Perplexing Protein Puzzles

    Författare :Stina Lindman; Biofysikalisk kemi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; calbindin D9k; split-GFP; protein G B1; pKa-values; protein reconstitution; Electrostatic interactions; protein stability; protein denaturation; heteronuclear NMR; pH titrations;

    Sammanfattning : Protein structure and stability are inherent in the amino acid sequence and governed by non-covalent interactions. The cooperation between forces is, however, perplexing and not well understood. In order to elucidate and predict protein folding and stability, detailed studies of non-covalent interactions are required. LÄS MER

  2. 2. Structure determination and thermodynamic stabilization of an engineered protein-protein complex

    Författare :Elisabet Wahlberg; Per-Åke Nygren; Bengt-Harald Jonsson; KTH; []
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; affibody; protein structure; coupled folding; NMR spectroscopy; protein stability; protein-protein interactions; binding thermodynamics; isothermal titration calorimetry; protein engineering; Structural biochemistry; Strukturbiokemi;

    Sammanfattning : The interaction between two 6 kDa proteins has been investigated. The studied complex of micromolar affinity (Kd) consists of the Z domain derived from staphylococcal protein A and the related protein ZSPA-1, belonging to a group of binding proteins denoted affibody molecules generated via combinatorial engineering of the Z domain. LÄS MER

  3. 3. Exploring small heat shock protein chaperones by crosslinking mass spectrometry

    Författare :Wietske Lambert; Biokemi och Strukturbiologi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; cross-linking; mass spectrometry; protein-protein interactions; Hsp21; BS3; DTSSP; MALDI-TOF TOF; client protein; substrate; aggregation; unfolded protein; chaperone; Small heat shock protein; crosslinking;

    Sammanfattning : Together with other molecular chaperones, small heat shock proteins are key components of the protein quality control system, which is comprised of several hundred proteins and acts to maintain proteome homeostasis in the cell. Small heat shock proteins bind unfolding proteins at an early stage, to prevent these from further unfolding and aggregating. LÄS MER

  4. 4. Structural and thermodynamical basis for molecular recognition between engineered binding proteins

    Författare :Jakob Dogan; Per-Åke Nygren; John E. Ladbury; KTH; []
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; protein structure; induced fit; binding thermodynamics; NMR spectroscopy; protein engineering; protein-protein interactions; protein stability; calorimetry; Structural biochemistry; Strukturbiokemi;

    Sammanfattning : The structural determination of interacting proteins, both as individual proteins and in their complex, complemented by thermodynamical studies are vital in order to gain in-depth insights of the phenomena leading to the highly selective protein-protein interactions characteristic of numerous life processes. This thesis describes an investigation of the structural and thermodynamical basis for molecular recognition in two different protein-protein complexes, formed between so-called affibody proteins and their respective targets. LÄS MER

  5. 5. Protein-protein interactions in model systems : design, control of catalytic activity and biosensor applications

    Författare :Johan Rydberg; Lars Baltzer; Joel Schneider; Linköpings universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Chemistry; Protein interactions; design; catalysis; biosensors; hybride materials; nanoparticles; Kemi; Chemistry; Kemi;

    Sammanfattning : This thesis describes the design of polypeptides, unordered in the monomeric state but capable of folding into helix-loop-helix motifs and dimerise to form four-helix bundles. The goal of the design was to encode them with the capacity to form dimers highly selectively and the ability to carry out molecular functions in the folded state but not in the unordered state, and thus to establish a molecular link between recognition and function. LÄS MER