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  • 1
    Keywords: Biochemistry ; Protein Science ; Springer eBooks
    Description / Table of Contents: Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation -- Ultrasensitive RT-QuIC Seed Amplification Assays for Disease-Associated Tau, α-Synuclein, and Prion Aggregates -- Vesicle-Based Assays to Study Membrane Interactions of Amyloid Peptides -- Differential Scanning Fluorimetry and Hydrogen Deuterium Exchange Mass Spectrometry to Monitor the Conformational Dynamics of NBD1 in Cystic Fibrosis -- A Multipronged Method for Unveiling Subtle Structural-Functional Defects of Mutant Chaperone Molecules Causing Human Chaperonopathies -- High-Throughput Microplate-Based Fluorescence Assays for Studying Stochastic Aggregation of Superoxide Dismutase-1 -- Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases -- Assays for Light Chain Amyloidosis Formation and Cytotoxicity -- Monitoring Aggregate Clearance and Formation in Cell-Based Assays -- Monitoring Proteome Stress in Live Cells Using HaloTag-Based Fluorogenic Sensor -- Quantification of Protein Aggregates Using Bimolecular Fluorescence Complementation -- Screening Protein Aggregation in Cells Using Fluorescent Labels Coupled to Flow Cytometry -- Induction of Cu/Zn Superoxide Dismutase (SOD1) Aggregation in Living Cells -- A Cell Model for HSP60 Deficiencies: Modeling Different Levels of Chaperonopathies Leading to Oxidative Stress and Mitochondrial Dysfunction -- Super-Resolution Fluorescence Imaging of Mutant Huntingtin Aggregation in Cells -- Thermal Shift and Stability Assays of Disease-Related Misfolded Proteins Using Differential Scanning Fluorimetry -- Methods to Screen Compounds against Mutant p53 Misfolding and Aggregation for Cancer Therapeutics -- Early Stage Discovery and Validation of Pharmacological Chaperones for the Correction of Protein Misfolding Diseases -- Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding -- In Vitro Prion Amplification Methodology for Inhibitor Screening -- SolubiS: Optimizing Protein Solubility by Minimal Point Mutations
    Abstract: This detailed book gathers a broad collection of experimental approaches to assist researchers in setting up different methods to investigate protein conformational disorders. Beginning with a section on assays focusing on biophysical approaches to study protein (mis)folding, the volume continues with sections on cellular and proteostasis assays as well as assays for protein folding correction and recovery, combining methods such as thermal shift assays, in silico improvement of protein solubility, and compound screening, an important area of research as it may open avenues for therapeutic strategies. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips for troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Misfolding Diseases: Methods and Protocols serves as an ideal guide for researchers seeking to advance our knowledge of protein conformational disorders
    Pages: XIII, 338 p. 77 illus., 58 illus. in color. : online resource.
    ISBN: 9781493988204
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  • 2
    ISSN: 1432-1327
    Keywords: Key words Ferredoxins ; Thermophiles ; Archaea ; EPR ; Iron-sulfur
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  Seven-iron ferredoxins from the thermoacidophilic archaea Acidianus ambivalens, A. infernus, Metalosphaera prunae and Sulfolobus metallicus were extensively characterised, allowing study of their expression under aerobic and anaerobic growth conditions as well as the putative role in thermal stability of a recently described zinc centre. The archaeon S. metallicus was found to express, under the same growth conditions, two ferredoxins in almost identical amounts, a novelty among Archaea. Most interestingly, these two ferredoxins differ at the N-terminal amino acid sequence in that one has a zinc binding motif (FdA) and the other does not (FdB); in agreement with these findings, FdA contains a zinc ion and FdB does not. These two ferredoxins have identical thermal stabilities, indicating that the zinc atom is not determinant in the protein thermostability. Further, the presence of the additional zinc centre does not interfere with the redox properties of the iron-sulfur clusters since their reduction potentials are almost identical. From the other three archaea, independently of the growth mode in respect to oxygen, only a single zinc-containing ferredoxin was found. EPR studies on the purified proteins, both in the oxidised and dithionite reduced states, allowed the identification of one [3Fe-4S]1+/0 centre and one [4Fe-4S]2+/1+ centre in all proteins studied. The complete sequence of A. ambivalens ferredoxin is reported. Together with the data gathered in this study, the properties of the seven-iron ferredoxins from Sulfolobales so far known are re-discussed.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Thiosulphate is one of the products of the initial step of the elemental sulphur oxidation pathway in the thermoacidophilic archaeon Acidianus ambivalens. A novel thiosulphate:quinone oxidoreductase (TQO) activity was found in the membrane extracts of aerobically grown cells of this organism. The enzyme was purified 21-fold from the solubilized membrane fraction. The TQO oxidized thiosulphate with tetrathionate as product and ferricyanide or decyl ubiquinone (DQ) as electron acceptors. The maximum specific activity with ferricyanide was 73.4 U (mg protein)−1 at 92°C and pH 6, with DQ it was 397 mU (mg protein)−1 at 80°C. The Km values were 2.6 mM for thiosulphate (kcat = 167 s−1),  3.4 mM  for  ferricyanide  and  5.87 µM for DQ. The enzymic activity was inhibited by sulphite (Ki = 5 µM), metabisulphite, dithionite and TritonX-100, but not by sulphate or tetrathionate. A mixture of caldariella quinone, sulfolobus quinone and menaquinone was non-covalently bound to the protein. No other cofactors were detected. Oxygen consumption was measured in membrane fractions upon thiosulphate addition, thus linking thiosulphate oxidation to dioxygen reduction, in what constitutes a novel activity among Archaea. The holoenzyme was composed of two subunits of apparent molecular masses of 28 and 16 kDa. The larger subunit appeared to be glycosylated and was identical to DoxA, and the smaller was identical to DoxD. Both subunits had been described previously as a part of the terminal quinol:oxygen oxidoreductase complex (cytochrome aa3).
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Desulfovibrio gigas is a strict anaerobe that contains a well-characterized metabolic pathway that enables it to survive transient contacts with oxygen. The terminal enzyme in this pathway, rubredoxin:oxygen oxidoreductase (ROO) reduces oxygen to water in a direct and safe way. The 2.5 Å ...
    Type of Medium: Electronic Resource
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