TY - JOUR
T1 - Chemical shifts in amino acids, peptides, and proteins
T2 - From quantum chemistry to drug design
AU - Oldfield, Eric
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2002
Y1 - 2002
N2 - This chapter discusses recent progress in the investigation and use of 13C, 15N, and 19F nuclear magnetic resonance (NMR) chemical shifts and chemical shift tensors in proteins and model systems primarily using quantum chemical (ab initio Hartree-Fock and density functional theory) techniques. Correlations between spectra and structure are made and the techniques applied to other spectroscopic and electrostatic properties as well, including hydrogen bonding, ligand binding to heme proteins, J-couplings, electric field gradients, and atoms-in-molecules theory, together with a brief review of the use of NMR chemical shifts in drug design.
AB - This chapter discusses recent progress in the investigation and use of 13C, 15N, and 19F nuclear magnetic resonance (NMR) chemical shifts and chemical shift tensors in proteins and model systems primarily using quantum chemical (ab initio Hartree-Fock and density functional theory) techniques. Correlations between spectra and structure are made and the techniques applied to other spectroscopic and electrostatic properties as well, including hydrogen bonding, ligand binding to heme proteins, J-couplings, electric field gradients, and atoms-in-molecules theory, together with a brief review of the use of NMR chemical shifts in drug design.
KW - Electrostatics
KW - Porphyrins
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U2 - 10.1146/annurev.physchem.53.082201.124235
DO - 10.1146/annurev.physchem.53.082201.124235
M3 - Article
C2 - 11972012
AN - SCOPUS:0036025444
SN - 0066-426X
VL - 53
SP - 349
EP - 378
JO - Annual Review of Physical Chemistry
JF - Annual Review of Physical Chemistry
ER -