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Do we see what we should see? Describing non-covalent interactions in protein structures including precision

Gurusaran, Manickam and Shankar, Mani and Nagarajan, Raju and Helliwell, John R and Sekar, Kanagaraj (2014) Do we see what we should see? Describing non-covalent interactions in protein structures including precision. In: IUCRJ, 1 (1). pp. 74-81.

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Official URL: http://dx.doi.org/10.1107/S2052252513031485


The power of X-ray crystal structure analysis as a technique is to `see where the atoms are'. The results are extensively used by a wide variety of research communities. However, this `seeing where the atoms are' can give a false sense of security unless the precision of the placement of the atoms has been taken into account. Indeed, the presentation of bond distances and angles to a false precision (i.e. to too many decimal places) is commonplace. This article has three themes. Firstly, a basis for a proper representation of protein crystal structure results is detailed and demonstrated with respect to analyses of Protein Data Bank entries. The basis for establishing the precision of placement of each atom in a protein crystal structure is non-trivial. Secondly, a knowledge base harnessing such a descriptor of precision is presented. It is applied here to the case of salt bridges, i.e. ion pairs, in protein structures; this is the most fundamental place to start with such structure-precision representations since salt bridges are one of the tenets of protein structure stability. Ion pairs also play a central role in protein oligomerization, molecular recognition of ligands and substrates, allosteric regulation, domain motion and alpha-helix capping. A new knowledge base, SBPS (Salt Bridges in Protein Structures), takes these structural precisions into account and is the first of its kind. The third theme of the article is to indicate natural extensions of the need for such a description of precision, such as those involving metalloproteins and the determination of the protonation states of ionizable amino acids. Overall, it is also noted that this work and these examples are also relevant to protein three-dimensional structure molecular graphics software.

Item Type: Journal Article
Publication: IUCRJ
Additional Information: Copy right for this article belongs to the INT UNION CRYSTALLOGRAPHY, 2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND
Keywords: salt bridges; crystal structure analysis; protein crystal structure precision; full-matrix least-squares method; measurement uncertainty; diffraction-component precision index; DPI; neutron diffraction
Department/Centre: Division of Interdisciplinary Sciences > Supercomputer Education & Research Centre
Date Deposited: 31 Jul 2015 14:30
Last Modified: 31 Jul 2015 14:30
URI: http://eprints.iisc.ac.in/id/eprint/51982

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