Structural and Dynamic Characterization of Artificially LinkedUbiquitin Dimers by NMR spectroscopy
نویسندگان
چکیده
منابع مشابه
Structural characterization of polyglutamine fibrils by solid-state NMR spectroscopy.
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides below, at, and above the toxicity limit of around 37 glutamine residues using solid-state NMR and electron microscopy. Experimental data are consistent with a dry fibril core of at least 70-80 Å ...
متن کاملStructural characterization of intrinsically disordered proteins by NMR spectroscopy.
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) which are in general highly flexible and do not have a well-defined secondary or tertiary structure under fu...
متن کاملStructural and dynamical characterization and binding investigation of Calpastatin by NMR spectroscopy Ph.D. theses
متن کامل
Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Here, we present a structural and dynamic description of CBP-ID4 at atomic resolution. ID4 is the fourth intrinsically disordered linker of CREB-binding protein (CBP). In spite of the largely disordered nature of CBP-ID4, NMR chemical shifts and relaxation measurements show a significant degree of α-helix sampling in the protein regions encompassing residues 2-25 and 101-128 (1852-1875 and 1951...
متن کاملStructural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy.
The phosphotriesterase from Pseudomonas diminuta catalyzes the hydrolysis of organophosphate esters. The isolated native protein contains zinc, and removal of this metal abolishes the enzymatic activity. Reconstitution of the apoenzyme requires 2 mol of cadmium per mol of protein for full catalytic activity. The kcat and Km values for the hydrolysis of paraoxon for the cadmium-substituted enzym...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: ChemBioChem
سال: 2019
ISSN: 1439-4227,1439-7633
DOI: 10.1002/cbic.201900146