When considering the structure of a protein, it is too easy to neglect the surrounding molecules that form the native habitat. This can be particularly detrimental when dealing with integral membrane proteins (IMPs), which are important medicinal targets. IMPs inhabit the cellular membrane. This means that they are entrenched in a combination of lipids and sugars, and undergo crucial hydrophobic and electrostatic interactions with membrane constituents. To probe these interactions, solid-state nuclear magnetic resonance spectroscopy (SSNMR) is used to study the surroundings of an integral membrane protein called Anabaena sensory rhodopsin (ASR). The process for identifying lipids and sugars that surround an IMP using SSNMR is demonstrated in the case of ASR. It is discovered that a disaccharide is tightly associated with ASR, and the potential functional significance of this molecule is described.
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