The role of unstructured extensions in the rotational diffusion properties of a globular protein: the example of the titin i27 module.

ABSTRACT: The possibility of predicting the overall shape of a macromolecule in solution from its diffusional properties has gained increasing importance in the structural genomic era. Here we explore and quantify the influence that unstructured and flexible regions have on the motions of a globular protein, a situation that can occur from the presence of such regions in the natural sequence or from additional tags. I27, an immunoglobulin-like module from the muscle protein titin, whose structure and properties are well characterized, was selected for our studies. The backbone dynamics and the overall tumbling of three different constructs of I27 were investigated using (15)N NMR relaxation collected at two (15)N frequencies (60.8 and 81.1 MHz) and fluorescence depolarization spectroscopy after labe

SUBMITTER: Nicastro G 

PROVIDER: S-EPMC1304461 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature