Add to ORKGChaperones are important in preventing protein aggregation and aiding protein folding. How chaperones aid protein folding remains a key question in understanding their mechanism. The possibility of proteins folding while bound to chaperones was reintroduced recently with the chaperone Spy, many years after the phenomenon was first reported with the chaperones GroEL and SecB. In this review, we discuss the salient features of folding while bound in the cases for which it has been observed and speculate about its biological importance and possible occurrence in other chaperones
Conserved families of molecular chaperones assist protein folding in the cell. Here we review the co...
The interaction between proteins is central not only to this thesis, but to most processes in the ce...
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides ...
Molecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured...
The biological functions of proteins are governed by their three-dimensional fold. Protein folding, ...
Molecular chaperones are a class of proteins that interact with the non-native conformations of othe...
The major classes of molecular chaperones have highly variable sequences, sizes, and shapes, yet the...
The long-standing view that polypeptide chains newly synthesized inside cells fold spontaneously to ...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
After the discovery of the need for extensive assistance in protein folding in the case of many nasc...
Two classes of chaperonins are known in all groups of organisms to participate in the folding of new...
Molecular chaperones assist de novo protein folding and facilitate the refolding of stress-denatured...
SummaryGroEL and GroES form a chaperonin nano-cage for single protein molecules to fold in isolation...
In this issue, we explore the assembly roles of protein chaperones, mainly through the portal of the...
<div><p>How chaperones interact with protein chains to assist in their folding is a central open que...
Conserved families of molecular chaperones assist protein folding in the cell. Here we review the co...
The interaction between proteins is central not only to this thesis, but to most processes in the ce...
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides ...
Molecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured...
The biological functions of proteins are governed by their three-dimensional fold. Protein folding, ...
Molecular chaperones are a class of proteins that interact with the non-native conformations of othe...
The major classes of molecular chaperones have highly variable sequences, sizes, and shapes, yet the...
The long-standing view that polypeptide chains newly synthesized inside cells fold spontaneously to ...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
After the discovery of the need for extensive assistance in protein folding in the case of many nasc...
Two classes of chaperonins are known in all groups of organisms to participate in the folding of new...
Molecular chaperones assist de novo protein folding and facilitate the refolding of stress-denatured...
SummaryGroEL and GroES form a chaperonin nano-cage for single protein molecules to fold in isolation...
In this issue, we explore the assembly roles of protein chaperones, mainly through the portal of the...
<div><p>How chaperones interact with protein chains to assist in their folding is a central open que...
Conserved families of molecular chaperones assist protein folding in the cell. Here we review the co...
The interaction between proteins is central not only to this thesis, but to most processes in the ce...
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides ...