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  2. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Since proteins typically aggregate upon denaturation (or form fibrils) the detected species size will go up. This is label-free and independent of specific residues in the protein or buffer composition. The only requirement is that the protein actually aggregates/fibrillates after denaturation and that the protein of interest has been purified.

  3. ICMJE recommendations - Wikipedia

    en.wikipedia.org/wiki/ICMJE_recommendations

    The ICMJE recommendations (full title, "Recommendations for the Conduct, Reporting, Editing, and Publication of Scholarly Work in Medical Journals") are a set of guidelines produced by the International Committee of Medical Journal Editors for standardising the ethics, preparation and formatting of manuscripts submitted to biomedical journals for publication. [1]

  4. Protein Engineering Design & Selection - Wikipedia

    en.wikipedia.org/wiki/Protein_Engineering_Design...

    Protein Engineering Design & Selection is a publication of Oxford University Press. Created in 1986, the Journal covers topics related the engineering , design and selection of proteins for use in biotechnology and therapy, and for understanding the fundamental link between protein sequence, structure, dynamics, function, and evolution.

  5. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  7. Polyacrylamide gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Polyacrylamide_gel...

    Picture of an SDS-PAGE. The molecular markers (ladder) are in the left lane. Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility.

  8. Radioimmunoprecipitation assay buffer - Wikipedia

    en.wikipedia.org/wiki/Radioimmunoprecipitation...

    Radioimmunoprecipitation assay buffer (RIPA buffer) is a lysis buffer used to lyse cells and tissue for the radio immunoprecipitation assay (RIPA). [1] [2] This buffer is more denaturing than NP-40 or Triton X-100 because it contains the ionic detergents SDS and sodium deoxycholate as active constituents and is particularly useful for disruption of nuclear membranes in the preparation of ...

  9. Proteomics (journal) - Wikipedia

    en.wikipedia.org/wiki/Proteomics_(journal)

    Proteomics is a peer-reviewed scientific journal covering topics including whole proteome analysis of organisms, protein expression profiling, disease, pharmaceutical, agricultural and biotechnological applications, and analysis of cellular systems, organelles and protein complexes.