Paramagnetic effects in NMR for protein structures and ensembles: Studies of metalloproteins |
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Institution: | 1. Magnetic Resonance Center (CERM), University of Florence, via Sacconi 6, Sesto Fiorentino, 50019, Italy;2. Department of Chemistry “Ugo Schiff”, University of Florence, via Della Lastruccia 3, Sesto Fiorentino, 50019, Italy;3. Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (CIRMMP), via Sacconi 6, Sesto Fiorentino, 50019, Italy;2. Department of Chemistry and Biochemistry, Denison University, Granville, OH 43023, USA;1. Laboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005 Paris, France;2. Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland;1. Dipartimento di Scienze e Tecnologie Agro-Alimentari, Alma Mater Studiorum – Università di Bologna, Piazza Goidanich 60, 47521 Cesena, Italy;2. Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine – CIRMMP, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy;3. CERM – Magnetic Resonance Center, Università Degli Studi di Firenze, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy;4. Dipartimento di Chimica, Università Degli Studi di Firenze, Via Della Lastruccia 3, 50019 Sesto Fiorentino, Italy |
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Abstract: | Paramagnetic effects on the NMR spectra are known to encode information on structure, electronic properties and dynamics hardly accessible with any other technique, especially in the field of biological systems. Paramagnetism-based restraints are conveniently used for the de novo determination of protein structures, the structural refinement starting from crystallographic models, and for the determination of the internal arrangement of domains with known structures. Conformational variability can also be profitably interrogated including the possibility of uncovering the presence of states with very low population. The recent advances in the quantum chemistry treatment of paramagnetic NMR effects has provided new momentum to the field, allowing for the refinement of protein structures at the metal coordination site to an unprecedented resolution. |
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