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Shape change in crystallization of biological macromolecules

Published online by Cambridge University Press:  04 May 2016

Peter G. Vekilov
Affiliation:
Department of Chemical and Biomolecular Engineering, University of Houston, USA; vekilov@uh.edu
Sungwook Chung
Affiliation:
School of Chemical and Biomolecular Engineering, Pusan National University, South Korea; sungwook.chung@pusan.ac.kr
Katy N. Olafson
Affiliation:
University of Houston, USA; katy_olafson@yahoo.com
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Abstract

Conformational changes, and the formation of densely packed ordered aggregates or crystals, are behaviors that profoundly affect the properties of a molecule. Using the example of biological macromolecules, we discuss two types of interactions between these two behaviors. First, we demonstrate that shape change may be driven by crystallization if the gain in crystallization free energy is sufficient to overcome the transition to an unfavorable molecular conformation. Hence, the crystal structures of flexible molecules may be a poor representation of their free-phase atomic arrangements. Second, molecules with conformational variability, such as proteins, may facilitate the nucleation of their crystals by forming dense liquid clusters enriched in domain-swapped or misassembled oligomers. In the clusters, the nucleation barrier is reduced due to the lower surface free energy of the crystal/dense liquid interface, and nucleation is significantly faster.

Type
Research Article
Copyright
Copyright © Materials Research Society 2016 

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