Multidimensional Structure–Activity Relationship of a Protein in Its Aggregated States

Abstract

Gleich und doch sehr verschieden: Je nach den verwendeten chemischen, physikalischen und biologischen Bedingungen bildet ein einziges Protein fünf strukturell verschiedene Aggregate (siehe die Elektronenmikroskopiebilder, Maßstäbe: 500 nm), die alle das Kreuz‐β‐Faltblatt‐Motiv enthalten. Die Aggregate unterscheiden sich in ihrer Affinität zu Adenosin‐5′‐triphosphat, Thioflavin T, DNA und Membranmimetika sowie in ihrem Effekt auf die Zellgängigkeit.

On the Possible Amyloid Origin of Protein Folds

“…72 This unfavorable statistic for soluble proteins is not likely to apply to amyloids since their structure can amplify a low affinity several-fold through repeat-induced cooperative interactions. 61,66 Conclusion In this synopsis, we have discussed some of the possible peptide folds from which the protein fold universe may have arisen. With our arguments coming out in favor of an amyloid CA fold, there is no obvious reason to definitively exclude the possibility that any of the folds discussed above is the CA fold.…”

“…43,61 Interestingly, several studies have shown that there has been an evolutionary selection against β-aggregation-prone In each polymorph, the Glu side chain (yellow) exists in only one of two favored conformations. As in (a), there is an energy barrier (e.g., steric clashes) that prevents an individual from changing conformation on its own.…”

“…Nonetheless, amyloids satisfy all of our stated requirements for a CA fold and additionally have the potential to store information, 70,71 self-replicate, 69 and support biologically relevant activities. 61 Amino Acid Sequence Length and the CA Fold: A Probability Argument…”

The elusive middle domain of Hsp104 and ClpB: Location and function

“…1a) [13–18]. These aggregates are typically disordered or amorphous in structure [19, 20]. Additionally, Hsp104 can directly remodel amyloid and this activity governs prion inheritance in yeast (Fig.…”

Chaperone networks in protein disaggregation and prion propagation

“…Protein aggregates display a remarkable structural variability, as seen in electron microscopy, depending on the nature of the involved protein and the stress conditions causing protein aggregation (Kawai-Noma et al, 2010;Wang et al, 2010). Heat-shock induced protein aggregates display a rather disordered or amorphous structure, potentially caused by the co-aggregation of a large diversity of differently misfolded protein species (Tyedmers et al, 2010).…”