Exclusively heteronuclear (13) C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDPs)
| Autor: | Noam Y. Haba, Roberta Pierattelli, Wolfgang Bermel, Isabella C. Felli, Ivano Bertini, M V Vasantha Kumar, Jordan H. Chill |
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| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
Carbon Isotopes Magnetic Resonance Spectroscopy Chemistry Organic Chemistry Proteins Nuclear magnetic resonance spectroscopy Intrinsically disordered proteins Biochemistry Resonance (particle physics) Amino acid Crystallography Protein structure Heteronuclear molecule Molecular Medicine Amino Acids Molecular Biology |
| Zdroj: | Chembiochem : a European journal of chemical biology. 13(16) |
| ISSN: | 1439-7633 |
| Popis: | Carbon-13 direct-detection NMR methods have proved to be very useful for the characterization of intrinsically disordered proteins (IDPs). Here we present a suite of experiments in which amino-acid-selective editing blocks are encoded in CACON- and CANCO-type sequences to give (13) C-detected spectra containing correlations arising from a particular type or group of amino acid(s). These two general types of experiments provide the complementary intra- and inter-residue correlations necessary for sequence-specific assignment of backbone resonance frequencies. We demonstrate the capabilities of these experiments on two IDPs: fully reduced Cox17 and WIP(C) . The proposed approach constitutes an independent strategy to simplify crowded spectra as well as to perform sequence-specific assignment, thereby demonstrating its potential to study IDPs. |
| Databáze: | OpenAIRE |
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