AbstractProgressive structuring and ultimately exclusion of water by hydrophobes surrounding backbone hydrogen bonds turn the latter into guiding factors of protein folding. Here we demonstrate that an arrangement of five hydrophobes yields an optimal hydrogen-bond stabilization. This motif is shown to be nearly ubiquitous in native folds
AbstractPure Gō models (where every native interaction equally stabilizes the folded state) have wid...
It is commonly accepted that water plays an essential role in determining both the stability of the ...
AbstractThe goal of this article is to summarize what has been learned about the major forces stabil...
AbstractProgressive structuring and ultimately exclusion of water by hydrophobes surrounding backbon...
ABSTRACT Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbo...
AbstractA few backbone hydrogen bonds (HBs) in native protein folds are poorly protected from water ...
The prediction of binding sites and the understanding of interfaces associated with protein complexa...
AbstractA judicious examination of an exhaustive PDB sample of soluble globular proteins of moderate...
Identifying the forces that drive proteins to misfold and aggregate, rather than to fold into their ...
AbstractA judicious examination of an exhaustive PDB sample of soluble globular proteins of moderate...
Soluble proteins must maintain backbone hydrogen bonds (BHBs) water-tight to ensure structural integ...
The hydrophobic effect drives the folding of proteins into their native states within cells by maxim...
AbstractThis study shows that intramolecular hydrogen bonding in proteins depends on the accessibili...
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globu...
AbstractThe goal of this article is to summarize what has been learned about the major forces stabil...
AbstractPure Gō models (where every native interaction equally stabilizes the folded state) have wid...
It is commonly accepted that water plays an essential role in determining both the stability of the ...
AbstractThe goal of this article is to summarize what has been learned about the major forces stabil...
AbstractProgressive structuring and ultimately exclusion of water by hydrophobes surrounding backbon...
ABSTRACT Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbo...
AbstractA few backbone hydrogen bonds (HBs) in native protein folds are poorly protected from water ...
The prediction of binding sites and the understanding of interfaces associated with protein complexa...
AbstractA judicious examination of an exhaustive PDB sample of soluble globular proteins of moderate...
Identifying the forces that drive proteins to misfold and aggregate, rather than to fold into their ...
AbstractA judicious examination of an exhaustive PDB sample of soluble globular proteins of moderate...
Soluble proteins must maintain backbone hydrogen bonds (BHBs) water-tight to ensure structural integ...
The hydrophobic effect drives the folding of proteins into their native states within cells by maxim...
AbstractThis study shows that intramolecular hydrogen bonding in proteins depends on the accessibili...
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globu...
AbstractThe goal of this article is to summarize what has been learned about the major forces stabil...
AbstractPure Gō models (where every native interaction equally stabilizes the folded state) have wid...
It is commonly accepted that water plays an essential role in determining both the stability of the ...
AbstractThe goal of this article is to summarize what has been learned about the major forces stabil...