Structural Transformations in Protein Crystals caused by controlled Dehydration

Salunke, DM and Veerapandian, B and R. Kodandapani, R and Vijayan, M (1985) Structural Transformations in Protein Crystals caused by controlled Dehydration. In: Journal of Bioscience, 8 (1-2). pp. 37-44.

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Abstract

Recent experiments in this laboratory on structural transformations caused by controlled dehydration of protein crystals have been reviewed. X-ray diffraction patterns of the following crystals have been examined under varying conditions of environmental humidity in the relative humidity range of 100-75%: a new crystal form of bovine pancreatic ribonuclease A grown from acetone solution in tris buffer (I), the well-known monoclinic form of the protein grown from aqueous ethanol (II), the same form grown from a solution of 2-methyl pentan-2,4-diol in phosphate buffer (III), tetragonal (IV), orthorhombic (V), monoclinic (VI) and triclinic (VII) hen egg white lysozyme, porcine 2 Zn insulin (VIII), porcine 4 Zn insulin (IX) and the crystals of concanavalin A(X). I, II, IV, V and VI undergo one or more transformations as evidenced by discontinuous changes in the unit cell dimensions, the diffraction pattern and the solvent content. Such water-mediated transformations do not appear to occur in the remaining crystals in the relative humidity range explored. The relative humidity at which the transformation occurs is reduced when 2-methyl pentan-2,4-diol is present in the mother liquor. The transformations are affected by the crystal structure but not by the amount of solvent in the crystals. The X-ray investigations reviewed here and other related investigations emphasize the probable importance of water-mediated transformations in exploring hydration of proteins and conformational transitions in them.

Item Type:	Journal Article
Publication:	Journal of Bioscience
Publisher:	Springer
Additional Information:	Copyright of this article belongs to Springer
Keywords:	Water-mediated transformations; environmental humidity; protein crystals; conformational transitions; protein hydration.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	12 Nov 2009 12:46
Last Modified:	19 Sep 2010 05:31
URI:	http://eprints.iisc.ac.in/id/eprint/20190

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