Hydrophobic Interactions Improve Selectivity to ERα for Benzothiophene SERMs

Structural Modulation of Oxidative Metabolism in Design of Improved Benzothiophene Selective Estrogen Receptor Modulators (SERMs)

Contribution of hydrophobic interactions to protein stability.

Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface protein from Borrelia burgdorferi (VlsE) with 341 residues, and two proteins previously studied in our laboratory, ribonu...

Hydrophobic interactions: an overview

We present an overview of the recent progress that has been made in understanding the origin of hydrophobic interactions. We discuss the different character of the solvation behaviour of apolar solutes at small and large length scales. We emphasize that the crossover in the solvation behaviour arises from a collective effect, which means that implicit solvent models should be used with care. We...

Urea's action on hydrophobic interactions.

For more than a century, urea has been commonly used as an agent for denaturing proteins. However, the mechanism behind its denaturing power is still not well understood. Here we show by molecular dynamics simulations that a 7 M aqueous urea solution unfolds a chain of purely hydrophobic groups which otherwise adopts a compact structure in pure water. The unfolding process arises due to a weake...

Importance of Hydrophobic Motif Interactions

INTRODUCTION The Serum and Glucocorticoid regulated kinases (SGK) are a family of serine/threonine protein kinases that show extensive sequence homology to the Protein Kinase B (PKB/Akt) enzymes. Three isoforms exist in humans: SGK1, SGK2 and SGK3. Like PKB, SGK1 acts downstream of phosphatidylinositol-3-kinase (PI3K) (1). PKB requires phosphorylation of its activation loop and of a hydrophobic...