ISBN: 9783319395340

This thesis presents a method for reliably and robustly producing samples of amyloid-ss (Ass) by capturing them at various stages of aggregation, as well as the results of subsequent imag… Mehr…

This thesis presents a method for reliably and robustly producing samples of amyloid-ss (Ass) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide's nanomechanical, elastic, thermal or spectroscopical properties. Amyloid-ss (Ass) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of Ass with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes. eBooks > Fremdsprachige eBooks > Englische eBooks > Sach- & Fachthemen > Technik; eBooks > Fremdsprachige eBooks > Englische eBooks > Sach- & Fachthemen > Biologie; eBooks > Fachbücher > Medizin; eBooks > Fremdsprachige eBooks > Englische eBooks > Sach- & , Springer, Springer<

ISBN: 9783319395340

This thesis presents a method for reliably and robustly producing samples of amyloid- (A) by capturing them at various stages of aggregation, as well as the results of subsequent imaging … Mehr…

This thesis presents a method for reliably and robustly producing samples of amyloid- (A) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide's nanomechanical, elastic, thermal or spectroscopical properties. Amyloid- (A) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of A with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.; PDF; Scientific, Technical and Medical > Medicine: general issues > Medical equipment & techniques > Medi, Springer International Publishing<

2016, ISBN: 9783319395340

This thesis presents a method for reliably and robustly producing samples of amyloid-ß (Aß) by capturing them at various stages of aggregation, as well as the results of subsequent imagin… Mehr…

This thesis presents a method for reliably and robustly producing samples of amyloid-ß (Aß) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide's nanomechanical, elastic, thermal or spectroscopical properties. Amyloid-ß (Aß) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of Aß with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes. eBook Claire Louisa Tinker-Mill PDF, Springer, 05.07.2016, Springer, 2016<

ISBN: 9783319395340

; PDF; Scientific, Technical and Medical > Medicine: general issues > Medical equipment & techniques > Medi, Springer Berlin Heidelberg

2016, ISBN: 9783319395340

eBooks, eBook Download (PDF), 1st ed. 2016, [PU: Springer International Publishing], Springer International Publishing, 2016