The intracellular environment represents an extremely crowded milieu, with a limited amount
of free water and an almost complete lack of unoccupied space. Obviously, slightly salted …

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 …

The formation of amyloid aggregates upon protein misfolding is related to several
devastating degenerative diseases. The propensities of different protein sequences to …

A typical casein micelle contains thousands of casein molecules, most of which form
thermodynamically stable complexes with nanoclusters of amorphous calcium phosphate …

Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

The abundant existence of proteins and regions that possess specific functions without
being uniquely folded into unique 3D structures has become accepted by a significant …

Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions
because disordered segments permit interaction with several proteins and hence the re-use …

Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under
physiological conditions in vitro. They are highly abundant in nature and their functional …

Copper is too redox active to exist in an unbound form in the cell without causing oxidative
damage: an upper limit of 10-18 M for the free concentration of Cu (II) in unstressed cells has …