Affiliation:
1. Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India
2. School of Advanced Sciences, Vellore Institute of Technology, Vellore, Tamil Nadu, India
Abstract
Abstract
Motivation
Protein–carbohydrate interactions perform several cellular and biological functions and their structure and function are mainly dictated by their binding affinity. Although plenty of experimental data on binding affinity are available, there is no reliable and comprehensive database in the literature.
Results
We have developed a database on binding affinity of protein–carbohydrate complexes, ProCaff, which contains 3122 entries on dissociation constant (Kd), Gibbs free energy change (ΔG), experimental conditions, sequence, structure and literature information. Additional features include the options to search, display, visualization, download and upload the data.
Availability and implementation
The database is freely available at http://web.iitm.ac.in/bioinfo2/procaff/. The website is implemented using HTML and PHP and supports recent versions of major browsers such as Chrome, Firefox, IE10 and Opera.
Contact
gromiha@iitm.ac.in
Supplementary information
Supplementary data are available at Bioinformatics online.
Funder
Department of Biotechnology, Government of India
Ministry of Human Resource and Development
India and the DST-INSPIRE
Publisher
Oxford University Press (OUP)
Subject
Computational Mathematics,Computational Theory and Mathematics,Computer Science Applications,Molecular Biology,Biochemistry,Statistics and Probability
Cited by
13 articles.
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