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Abstract:
Solvent accessibility is a key property of proteins to characterize
them at each amino acid location within a chain. It plays crucial
role on protein-protein, protein-dna and protein-ligand interactions
as well as determining the stability of protein structures. Due
to a large gap in the number of available 3D structures of proteins
and due to a need to summarize the 3D structure in the form of local
and global descriptors, there is a pressing need to accurately predict
solvent accessibility of proteins from their sequence information.
We have extensively worked in this area and made several advances
in the field of predicting solvent accessibility from amino acid
sequence. I will review my key contributions to this subject and
present some ongoing work in this direction.
Biodata
of Speaker:
Dr
Shandar Ahmad obtained Doctor of Philosophy in (computational condensed
matter) Physics in 1994 from Department of Physics, Jamia Millia
Islamia (Central University), India. After graduation he joined
Department of Biosciences, Jamia Millia Islamia University as a
lecturer, where he is a Reader now. He has been a visiting scientist
with Department of Bioscience and Bioinformatics, Kyushu Institute
of Technology, Japan. He has recently published research papers
in the field of bioinformatics in high impact factor journals and
developed a number of scientific software, which are made available
online on his website www.netasa.org. This site provides links to
online tools for prediction/ analysis of different aspects of biological
systems, developed by Dr Shandar and colleagues.
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