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Analysis of Soluble Sugar Permease Domains by Solution NMR

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Knowledge of membrane transporter molecular structures is crucial for obtaining a detailed understanding of the mechanism by which these proteins shuttle their cargo across a biological membrane. Unfortunately, ascertaining complete structures of these transporters currently poses a difficult challenge for the structural biologist, as whole membrane proteins are generally refractory to analyses by X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. The hydrophobic nature of these proteins leads to aggregation that represents a barrier to crystallization; similarly, the aggregation properties of these proteins in solution thwart efforts to collect high-quality NMR spectra. Nonetheless, NMR spectroscopy does provide some experimental avenues for characterizing membrane transporter structure and function. Membrane transporters frequently take on a modular structure, being organized into cytoplasmic and integral membrane domains that perform distinct functions. The soluble cytoplasmic domains of a number of sugar permeases have been studied extensively using various solution NMR techniques (1 6 ), and NMR methodologies applied toward such studies will be described in this chapter. In addition, solid-state NMR has been employed to examine the conformation of transmembrane segments in lipid environments; descriptions of such studies are provided elsewhere in this volume (see Chapter 16 ).
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