The importance of sequence diversity in the aggregation and evolution of proteins

Article Abstract:

Incorrect folding of proteins, leads to aggregation and amyloid formation associated with diseases like Alzheimer's and late onset diabetes. Aggregation kinetics of multidomain protein constructs of immunoglobulins is described and it is shown that aggregation of these proteins is a specific process and that the efficiency of coaggregation between different domains decreases with decreasing sequence identity.

Analysis, Alzheimer's disease, Protein folding, Amino acid sequence, Amino acid sequencing

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Prying into prions

Article Abstract:

The relationship between specific structural features and biological properties such as infectivity is established using the 71-residue carboxyl-terminal region of a prion, known as HET-s, from a filamentous fungus. Four regions of the sequence are identified as being involved in beta-sheet structure using nuclear magnetic resonance techniques.

Filamentous bacteria

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Correlation of structural elements and infectivity of the HET-s prion

Article Abstract:

The sequence-specific positions of amyloid fibril secondary structure elements of HET-s(218-289) are determined by using fluorescence studies, quenched hydrogen exchange NMR and solid-state NMR. This approach revealed four bet-strands constituted by two pseudo-repeat sequences, each forming a beta-strand-turn-beta-strand motif.

Glycoproteins

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