Non-native architectures in protein design and mimicry
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A review. Topics include pseudo-prolines (YPro) as a solubilizing, structure-disrupting protection technique in peptide synthesis and the concept of Template-Assembled-Synthetic Proteins (TASP). [on SciFinder (R)] ...
Recently, a new method for the specific covalent labeling of fusion proteins in vitro and in living cells has been developed. This method is based on the unusual mechanism of a DNA repair protein: the O6-alkylguanine DNA alkyltransferase (AGT). In addition ...
During protein folding a polypeptide chain has to form specific intrachain interactions starting from an ensemble of unfolded conformation. Thus, intrachain diffusion in unfolded polypeptide chains can be regarded as an elementary step in protein folding, ...
Fusion proteins of human O6-alkylguanine-DNA alkyltransferase (AGT) can be specifically labeled with a wide variety of synthetic probes in mammalian cells; this makes them an attractive tool for studying protein function. However, to avoid undesired labeli ...
Intrachain diffusion processes play an important role in protein folding and function. In this chapter we discuss the application of triplet-triplet energy transfer to directly measure rate constants for intrachain contact formation in polypeptide chains. ...
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HypA and HypB are maturation proteins required for incorporation of nickel into the hydrogenase large subunit. To examine the functions of these proteins in nickel insertion, the hybF gene, which is a homolog of hypA essential for maturation of hydrogenase ...
The selective and reversible insertion of pseudo-proline (PsiPro) Systems in cyclosporin C (CsC) featuring different C(2) substituents at the oxazolidine ring and its impact on the conformational and biological properties is described. The presence of a 5- ...
The description at at. level of protein folding is an ambitious goal in biophysics, particularly because of the difficulty in obtaining structural information on unfolded states. Computer simulations can contribute in achieving this goal. Here we report th ...
The rate of formation of intramolecular interactions in unfolded proteins determines how fast conformational space can be explored during folding. Characterization of the dynamics of unfolded proteins is therefore essential for the understanding of the ear ...
