Rapid biophysical characterization and NMR structural analysis of small proteins from bacteria and archaea.

Rapid biophysical characterization and NMR structural analysis of small proteins from bacteria and archaea. Chembiochem. 2019 Nov 09;: Authors: Kubatova N, Pyper DJ, Jonker HRA, Saxena K, Remmel L, Richter C, Brantl S, Evguenieva-Hackenberg E, Hess W, Klug G, Marchfelder A, Soppa J, Streit W, Mayzel M, Orekhov VY, Fuxreiter M, Schmitz-Streit R, Schwalbe H Abstract Proteins encoded by small open reading frames (sORFs) have a widespread occurrence in diverse microorganisms and can be of high functional importance. However, due to annotation biases and their technically challenging direct detection, these small proteins were overlooked for a long time and are becoming discovered only recently. The currently rapidly growing number of such proteins requires efficient methods to investigate their structure-function-relation. Here, we present a method for fast determination of the conformational properties of small proteins. Their small size makes them perfectly amenable for solution-state NMR spectroscopy. NMR spectroscopy can provide detailed information about their conformational states (folded, partially folded and unstructured). In the context of the priority program on small proteins funded by the German research foundation (SPP2002), we have investigated 27 small proteins from nine different bacterial and archaeal organisms. We found that most of these small proteins are unstructured or partially folded. Bioinformatics tools predict ...
Source: Chembiochem - Category: Biochemistry Authors: Tags: Chembiochem Source Type: research