title: 15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli.
abstract: In the solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli in the free state two structural segments can be distinguished: a well structured, rigid N-terminal part displaying a betaalphabetabetabetaalpha topology and a flexible C-terminal tail comprising last 20 amino-acid residues. The backbone dynamics of Yfia protein was studied by (15)N nuclear magnetic relaxation at three magnetic fields and analyzed using model-free approach. The overall diffusional tumbling of the N-terminal part is strongly anisotropic with a number of short stretches showing increased mobility either on a subnanosecond time scale, or a micro- to millisecond time scale, or both. In contrast, the unstructured polypeptide chain of the C-terminal part, which cannot be regarded as a rigid structure, shows the predominance of fast local motions over slower ones, both becoming faster closer to the C-terminus.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland.
authors.forename: Igor
authors.initials: I
authors.lastname: Zhukov
authors.forename: Peter
authors.initials: P
authors.lastname: Bayer
authors.forename: Beate
authors.initials: B
authors.lastname: Schölermann
authors.forename: Andrzej
authors.initials: A
authors.lastname: Ejchart
mesh_terms: D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D009587:Nitrogen Isotopes / Q000737:chemistry; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; C434525:RaiA protein, E coli; D012269:Ribosomal Proteins