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Toward the quantum chemical calculation of nuclear magnetic resonance chemical shifts of proteins
Author(s) -
Frank Andrea,
Onila Ionut,
Möller Heiko M.,
Exner Thomas E.
Publication year - 2011
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.23041
Subject(s) - chemical shift , quantum chemical , nuclear magnetic resonance spectroscopy , chemistry , measure (data warehouse) , nuclear magnetic resonance , computational chemistry , chemical physics , molecule , physics , computer science , data mining , organic chemistry
Despite the many protein structures solved successfully by nuclear magnetic resonance (NMR) spectroscopy, quality control of NMR structures is still by far not as well established and standardized as in crystallography. Therefore, there is still the need for new, independent, and unbiased evaluation tools to identify problematic parts and in the best case also to give guidelines that how to fix them. We present here, quantum chemical calculations of NMR chemical shifts for many proteins based on our fragment‐based quantum chemical method: the adjustable density matrix assembler (ADMA). These results show that 13 C chemical shifts of reasonable accuracy can be obtained that can already provide a powerful measure for the structure validation. 1 H and even more 15 N chemical shifts deviate more strongly from experiment due to the insufficient treatment of solvent effects and conformational averaging. Proteins 2011; © 2011 Wiley‐Liss, Inc.