Quantum chemical 13C chemical shift calculations for protein NMR structure determination, refinement, and validation
نویسندگان
چکیده
منابع مشابه
Quantum chemical 13C(alpha) chemical shift calculations for protein NMR structure determination, refinement, and validation.
A recently determined set of 20 NMR-derived conformations of a 48-residue all-alpha-helical protein, (PDB ID code 2JVD), is validated here by comparing the observed (13)C(alpha) chemical shifts with those computed at the density functional level of theory. In addition, a recently introduced physics-based method, aimed at determining protein structures by using NOE-derived distance constraints t...
متن کاملNMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination.
In this tutorial review, we discuss the utilization of chemical shift information as well as ab initio calculations of nuclear shieldings for protein structure determination. Both the empirical and computational aspects of the chemical shift are reviewed and the role of molecular dynamics and the accuracy of different computational methods are discussed. It is anticipated that incorporating the...
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NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural c...
متن کامل13C and chemical shift referencing in biomolecular NMR
~Protein Engineering Network of Centres of Excellence, Department of Biochemistry, University of Alberta, Edmonton, AB, Canada T6G 2S2 bDepartment of Molecular Biology, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, CA 92037, US.A. "National Magnetic Resonance Facility at Madison, Department of Biochemistry, University of Wisconsin at Madison, 420 Henry Mall, Madison, ...
متن کاملSolid-State NMR Determination of 13CR Chemical Shift Anisotropies for the Identification of Protein Secondary Structure
A solid-state nuclear magnetic resonance (NMR) method for the site-resolved identification of the secondary structure of solid peptides and proteins is presented. This technique exploits the correlation between the backbone conformation and the CR chemical shift anisotropies (CSA) of proteins. The 13CR CSAs are measured under fast magic-angle-spinning using a new sequence of sixteen 180° pulses...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2008
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0807105105