Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …

General principles of protein structure, stability, and folding kinetics have recently been
explored in computer simulations of simple exact lattice models. These models represent …

Publisher Summary This chapter describes the present state of the studies of the molten
globule state and its role in protein folding and physiological processes. Recent data on the …

To establish a framework for extrapolating the helix-forming properties of peptides from
TFE/H2O mixtures (TFE= 2, 2, 2-trifluoroethanol) back to water, the thermal unfolding curves …

Parkinson's disease involves the loss of dopaminergic neurons in the substantia nigra,
leading to movement disorders. The pathological hallmark of Parkinson's disease is the …

Preparation of biological macromolecules in the pure state requires that cells be disrupted,
releasing and mixing the contents. Only the most stable and highly structured molecules can …

Intrinsically disordered proteins (IDPs) differ from “normal” ordered proteins at several levels,
structural, functional and conformational. Amino acid biases characteristic for IDPs …

Trifluoroethanol (TFE) is known to stabilize the α-helical structure in proteins and their
fragments. However, the relationship between the TFE-induced structures and the native …

Among various alcohols, those substituted with fluorine, such as 2, 2, 2-trifluoroethanol
(TFE) or 3, 3, 3, 3 ', 3 ', 3 '-hexafluoro-2-propanol (HFIP), have a marked potential to induce …

Limited proteolysis is responsible for activating a wide range of proteins from immature
forms and is hence implicated in a number of biologically imporw x tant systems 1–3 …