Read e-book online Amyloid, Prions, and Other Protein Aggregates, Part C PDF

By Ronald Wetzel, Indu Kheterpal

The facility of polypeptides to shape on the other hand folded, polymeric constructions akin to amyloids and comparable aggregates is being more and more well-known as a massive new frontier in protein learn. This new quantity of equipment in Enzymology in addition to half B (volume 412) on Amyloid, Prions and different Protein Aggregates proceed within the culture of the 1st quantity (309) in containing specific protocols and methodological insights, supplied through leaders within the box, into the most recent equipment for investigating the constructions, mechanisms of formation, and organic actions of this crucial category of protein assemblies.

* offers precise protocols
* contains troubleshooting suggestions
* presents insurance on structural biology, computational tools, and biology

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Additional info for Amyloid, Prions, and Other Protein Aggregates, Part C

Sample text

5. Disaggregated peptide should normally be prepared fresh, because aggregates build up even when the peptide is stored at À80 . , 2002a) (see section on preparation of stocks of aggregate seeds). Thus, snap‐freeze in dry ice and ethanol or liquid nitrogen, and store at À80 . It may be possible to remove trace aggregates from stored samples by 42 amyloid, prions, and other protein aggregates, part C [3] repeating the centrifugation step after thawing. If this is done, it may be advisable to redetermine the peptide concentration in the supernatant.

The various elements include: (1) disaggregation of peptides prior to initiation of aggregation, [3] kinetics and thermodynamics of amyloid assembly 37 (2) preparation of seeds for use in elongation studies, (3) the basic HPLC sedimentation assay, (4) determination of the average functional molecular weight of an aggregate population, (5) elongation kinetics, (6) nucleation kinetics, and (7) thermodynamics of amyloid fibril elongation. The chapter is necessarily lengthy, and it might be argued that it could have been divided into multiple chapters.

The polyGln peptides also exhibit a wide range of amyloid‐like aggregate morphologies, many of which are capable of seeding aggregate growth [3] kinetics and thermodynamics of amyloid assembly 45 by monomer addition. , 2002a). , 2002a). Longer polyGln sequences favor amyloid fibril formation, as do the low‐salt growth conditions that tend to slow down aggregate assembly. Formation of protofibril‐like structures requires the unusual growth condition of freezing a PBS solution in the À20 to À5 range.

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