NACDDB - The Web Server for DNA,RNA,and Hybrids Circular Dichroism Structure

Capturing, sharing and analysing biophysical data from protein engineering and protein characterization studies

Overview of Farrell D et al.

AuthorsFarrell D  O'Meara F  Johnston M  Bradley J  Søndergaard CR  Georgi N  Webb H  Tynan-Connolly BM  Bjarnadottir U  Carstensen T  Nielsen JE  
AffiliationCentre for Synthesis and Chemical Biology   School of Biomolecular and Biomedical Science   UCD Conway Institute   University College Dublin   Belfield   Dublin 4   Ireland.  
JournalNucleic Acids Res
Year 2010

Abstract


Large amounts of data are being generated annually on the connection between the sequence, structure and function of proteins using site-directed mutagenesis, protein design and directed evolution techniques. These data provide the fundamental building blocks for our understanding of protein function, molecular biology and living organisms in general. However, much experimental data are never deposited in databases and is thus 'lost' in journal publications or in PhD theses. At the same time theoretical scientists are in need of large amounts of experimental data for benchmarking and calibrating novel predictive algorithms, and theoretical progress is therefore often hampered by the lack of suitable data to validate or disprove a theoretical assumption. We present PEAT (Protein Engineering Analysis Tool), an application that integrates data deposition, storage and analysis for researchers carrying out protein engineering projects or biophysical characterization of proteins. PEAT contains modules for DNA sequence manipulation, primer design, fitting of biophysical characterization data (enzyme kinetics, circular dichroism spectroscopy, NMR titration data, etc.), and facilitates sharing of experimental data and analyses for a typical university-based research group. PEAT is freely available to academic researchers at http://enzyme.ucd.ie/PEAT.