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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
COILCHECK: an interactive server for the analysis of interface regions in coiled coils
V Alva1, D P Syamala Devi, R Sowdhamini
1Institute of Bioinformatics and Applied Biotechnology, G-05, Tech Park Mall, Internatioonal Technology Park Bangalore, Whitefield Road, Bangalore 560 066, India.
Abstract:
Coiled coils are important structural modules and domains of protein-protein interactions. Further, they provide the required framework to proteins, like kinesins, myosins and SNAREs, which are either structural or involved in transport of biomolecules. We provide an interactive webserver to measure the strength of interactions between two helices involved in coiled coils. Interactions are measured using non-bonded and electrostatic interactions and the presence of hydrogen bonds and salt bridges. The sum of these interactions is expressed as psuedoenergy, whose ranges have been standardized using all structural entries that are classified to contain coiled coils. The results are displayed conveniently as energy per residue along with options to obtain detailed list of different types of interactions. This webserver can be useful to assess the strength of coiled coil regions, to recognize weak and strong regions, to rationalize the phenotypic behaviour of single residue mutations as well as to design mutation experiments. COILCHECK webserver can be accessed from http://caps.ncbs.res.in/coilcheck/.
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