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We present a method of assessing the quality of protein structures based on the use of side-chain NMR chemical shifts. Because these parameters are very accurate reporters of side-chain positions and are highly sensitive to tertiary structure and packing, they are particularly useful for structure validation. To analyze a given structure, we define a quality score, QCS, that compares the chemical shifts calculated from such a structure with the corresponding experimental values in a way that takes account of the errors in the calculations. The results that we report illustrate the advantages in the examination of the quality of protein structures from the perspective of side-chains.

Original publication

DOI

10.1021/jp2122054

Type

Journal article

Journal

J Phys Chem B

Publication Date

26/04/2012

Volume

116

Pages

4754 - 4759

Keywords

Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Proteins