Charge interactions can dominate the dimensions of intrinsically disordered proteins

Abstract

The authors note that on page 4454, left column, 2nd full paragraph, lines 7-9, "For example, oxidation catalysts are able to reduce N 2 O emissions ∼70% compared with models without the technology (22)" should instead appear as "For example, advanced three-way catalysts are able to reduce N 2 O emissions ∼65% compared with models without the technology (22)."

Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH

“…1(b)). This effect has been observed for a broad variety of proteins and peptides 2,4,8,9,[12][13][14]35 and can be described as a continuous expansion of the chain on transfer to good solvent. 25 The interesting question here is how mixtures of denaturants 36 and drastic changes in pH will affect the dimensions of the unfolded state.…”

“…Understanding protein folding 1, 2 and the functional properties of intrinsically disordered proteins (IDPs) [3][4][5] requires detailed knowledge of the forces that act in unstructured polypeptide chains. These forces determine the dimensions of unfolded and disordered proteins and have been suggested to impact processes such as the coupled binding and folding of IDPs, 5 or the rate of protein folding reactions.…”

“…These forces determine the dimensions of unfolded and disordered proteins and have been suggested to impact processes such as the coupled binding and folding of IDPs, 5 or the rate of protein folding reactions. [6][7][8] However, the dimensions of unfolded proteins and IDPs also depend critically on solution conditions such as ionic strength, 4,9 temperature, 10 osmolytes, 11 or denaturants, 2,[12][13][14] implying that the complex interplay between chain-chain and chainsolvent interactions has to be unraveled before quantitative predictions of the size of unstructured polypeptide chains and their effect on folding or binding will be possible.…”

“…4,[12][13][14] However, a prerequisite for their application is knowledge of the -state, which serves as a reference state for the coil-to-globule transition. At thepoint, chain-chain and chain-solvent interactions balance, and the chain obeys the length scaling of an ideal chain.…”

Reconfiguration dynamics in folded and intrinsically disordered protein with internal friction: Effect of solvent quality and denaturant

“…Higher the denaturant concentration lower the internal friction. On the other hand for an intrinsically disordered protein (IDP) such as C-terminal segment of human prothymosin α (ProTα) magnitude of internal friction is smaller [71,72] and at high denaturant concentration it is negligibly small. This is presumably due to exposed hydrophilic and charged residues resulting expansion of the protein.…”