It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …

Abstract “Natively unfolded” proteins occupy a unique niche within the protein kingdom in
that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino …

Irreversible protein aggregation is problematic in the biotechnology industry, where
aggregation is encountered throughout the lifetime of a therapeutic protein, including during …

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, eg to
characterize folding intermediates, measure surface hydrophobicity, and detect aggregation …

Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding
aggregates. Substantial data support the hypothesis that partially folded intermediates are …

In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril
formation were studied under different conditions using the fluorescent dye thioflavin T …

Parkinson's disease involves the aggregation of α-synuclein to form fibrils, which are the
major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in …

Carbonic anhydrase (CA, EC 4.2. 1.1) is a protein that is especially well-suited to serve as a
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …

Natively unfolded or intrinsically unstructured proteins constitute a unique group of the
protein kingdom. The evolutionary persistence of such proteins represents strong evidence …