MPIbpc News mai06zwei.indd

Abstract

Introduction The structure of water-soluble proteins forms around a cluster of hydrophobic residues which avoid contact with the solvent, thus exposing most charged and polar amino acids to the aqueous interface. This effect is known as ‚hydrophobic collapse‘, and it is for this reason that the shape of many soluble proteins can very roughly be described as globular. A class of soluble proteins that has recently caught increased attention among structural biologists and biophysicists are α-helical repeat proteins, which fall somewhat outside of this rule. These proteins are formed from repeating arrangements of helix-loop-helix motifs, stacked to form large curved or superhelical structures (Fig. 1 A,B). Depending on their sequence and internal structure, the building blocks are called leucine-rich repeats (LRR), armadillo repeats, or HEAT-repeats; these building blocks form proteins such as nuclear transport receptors (karyopherins), clathrin, catenin, internalin, and ankyrin. As can be seen in Fig. 1A, their hydrophobic core is far from being globular, and due to the large hydrophilic surface area, these proteins are well suited for processes Inhalt

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Cite this paper

@inproceedings{Zachariae2006MPIbpcNM, title={MPIbpc News mai06zwei.indd}, author={Ulrich Zachariae and Helmut Grubm{\"{u}ller}, year={2006} }