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Five-dimensional crystallography probes molecular structure

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Posted November 27, 2013
Five-dimensional crystallography probes molecular structure
Structures of the intermediates IT, ICT, pR2, pB1 and the dark resting state of photoactive yellow protein on the main reaction pathway. Barriers of activation between the intermediates are determined by 5-D crystallography.
Successful development of new pharmaceuticals could be the payoff from five-dimensional crystallography, a new experimental technique employed by researchers carrying out studies at the BioCARS facility at the U.S. Department of Energy Office of Science’s Advanced Photon Source (APS).

X-ray crystallography uses x-rays to investigate protein structure, and has played an increasingly important role in drug discovery in recent decades. This technique essentially represents a type of extremely high-resolution microscopy for investigating the molecular structure of proteins with near-atomic resolution. This facilitates improved understanding of their function, and provides vital structural information on specific protein targets. In this way it can contribute to the design of new drugs that target specific proteins, or to the engineering of enzymes for specific industrial processes.

Protein folding is the process by which a protein takes on a specific three-dimensional (3-D) structure essential for it to function. Many proteins, called enzymes, promote or catalyze specific chemical reactions. The 3-D structures of these proteins change during the course of the reactions. Free energy landscapes represent multidimensional hyper-surfaces that determine the progress of catalyzed reactions, and characterization of these landscapes allows the reaction to be described and visualized.

In time-resolved crystallography (TRX), x-ray diffraction by crystals is utilized to examine in real time the structures of proteins as they are changing and therefore improve understanding of their function and gain important structural information on specific protein targets.

Read more at: Phys.org

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