Amyloid Prions and Other Protein Aggregates by Ronald Wetzel, Indu Kheterpal

By Ronald Wetzel, Indu Kheterpal

The power of polypeptides to shape however folded, polymeric buildings resembling amyloids and comparable aggregates is being more and more famous as an incredible new frontier in protein study. This new quantity of Methods in Enzymology besides half B (volume 412) on Amyloid, Prions and different Protein Aggregates proceed within the culture of the 1st quantity (309) in containing exact protocols and methodological insights, supplied by means of leaders within the box, into the most recent equipment for investigating the buildings, mechanisms of formation, and organic actions of this significant type of protein assemblies.

  • Presents targeted protocols
  • Includes troubleshooting tips
  • Provides insurance on structural biology, computational tools, and biology

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We found that the inclusion of this step had a significant positive impact on the quality of the purified protein product. We also inactivated trace amounts of proteases during experiments by the addition of specific protease inhibitors. Finally, we also describe initial structural and functional analyses that confirm the integrity of the purified protein. Introduction Polyglutamine diseases have attracted growing interest in recent years as protein misfolding disorders. , 1995). 1 Michelle K. M.

RNA Polymerases and Associated Factors (Part D) Edited by SANKAR L. ADHYA AND SUSAN GARGES VOLUME 372. Liposomes (Part B) Edited by NEJAT DU¨ZGU¨NES, VOLUME 373. Liposomes (Part C) Edited by NEJAT DU¨ZGU¨NES, VOLUME 374. Macromolecular Crystallography (Part D) Edited by CHARLES W. , AND ROBERT W. SWEET VOLUME 375. Chromatin and Chromatin Remodeling Enzymes (Part A) Edited by C. DAVID ALLIS AND CARL WU VOLUME 376. Chromatin and Chromatin Remodeling Enzymes (Part B) Edited by C. DAVID ALLIS AND CARL WU VOLUME 377.

And Pittman, R. N. (2003). The polyglutamine neurodegenerative protein ataxin‐3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 12, 3195–3205. , Berke, S. , Cohen, R. , and Paulson, H. L. (2004). Poly‐ubiquitin binding by the polyglutamine disease protein ataxin‐3 links its normal function to protein surveillance pathways. J. Biol. Chem. 279, 3605–3611. , Hamilton, J. , and Wetzel, R. (2002a). Amyloid‐like features of polyglutamine aggregates and their assembly kinetics.

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Amyloid Prions and Other Protein Aggregates by Ronald Wetzel, Indu Kheterpal
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