Abstract
The determination of macromolecular structures in anisotropic environments such as membranes is vital to the field of structural biology. While solid state nuclear magnetic resonance spectroscopy (SSNMR) methods have been demonstrated for obtaining three dimensional structures of membrane bound polypeptides (Cross and Opella, 1983; Ketchem et al, 1993; Opella et al, 1987), computational refinement methods are needed for optimally utilizing these constraints in such a molecular environment. Methods for structural determination and refinement of macromolecules in solution have fully evolved (Briinger et al, 1986; Clore et al, 1985; Havel and Wüthrich, 1985), but the nature of the constraints obtained for membrane proteins are such that a new refinement procedure must be developed. Described here is such a technique that has the ability to optimize the structure of a membrane protein in order to best represent the experimental data and determine its high-resolution structure.
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© 1996 Birkhäuser Boston
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Ketchem, R.R., Roux, B., Cross, T.A. (1996). Computational Refinement Through Solid State NMR and Energy Constraints of a Membrane Bound Polypeptide. In: Merz, K.M., Roux, B. (eds) Biological Membranes. Birkhäuser Boston. https://doi.org/10.1007/978-1-4684-8580-6_10
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DOI: https://doi.org/10.1007/978-1-4684-8580-6_10
Publisher Name: Birkhäuser Boston
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