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Comparison of the accuracy of protein solution structures derived from conventional and network‐edited NOESY data
Author(s) -
Hoogstraten Charles G.,
Choe Soheui,
Westler William M.,
Markley John L.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041106
Subject(s) - heteronuclear molecule , two dimensional nuclear magnetic resonance spectroscopy , nuclear overhauser effect , block (permutation group theory) , chemistry , spin diffusion , simulated annealing , crystallography , biological system , physics , nuclear magnetic resonance spectroscopy , algorithm , diffusion , computer science , stereochemistry , mathematics , geometry , thermodynamics , biology
Network‐editing experiments are variants of the basic NOESY experiment that allow more accurate direct measurement of interproton distances in macromolecules by defeating specific spin‐diffusion pathways. Two network‐editing approaches, block‐decoupled NOESY and complementary‐block‐decoupled‐NOESY, were applied as three‐dimensional, heteronuclear‐edited experiments to distance measurement in a small protein, turkey ovomucoid third domain (OMTKY3). Two‐hundred and twelve of the original 655 distance constraints observed in this molecule (Krezel AM et al., 1994, J Mol Biol 242 :203–214) were improved by their replacement by distances derived from network‐edited spectra, and distance geometry/simulated annealing solution structure calculations were performed from both the unimproved and improved distance sets. The resulting two families of structures were found to differ significantly, the most important differences being the hinge angle of a β‐turn and an expansion of the sampled conformation space in the region of the reactive‐site loop. The structures calculated from network‐editing data are interpreted as a more accurate model of the solution conformation of OMTKY3.