Biao Fu


Biao Fu graduated in Bioinformatics and Molecular Modeling at College of Biological Sciences, China Agricultural University, with a thesis concerning phylogenetic analysis of biological sequences, where meanwhile he acquired a minor major in Computer Sciences. He then moved to Beijing Genomics Institute, China Academy of Sciences, and worked as an employee in fields of genome data analysis and scientific programming for two years. Thereafter, Biao continued his studies at Finnish Biological NMR Center, University of Helsinki, on topics of methodological study of NMR spectroscopy, structure determination and analysis of molecule Follistatin FS Repeat 1 (FSD1). And that is what his master's thesis was written about. Biao demonstrated to be a competent student in field of biophysics and molecular biology. He has been appointed by University of Cambridge within the IDPbyNMR project.



Biao Fu
Project Topic
Rational drug design on IDPs using NMR-derived structural ensembles
Project Description
Molecular dynamics simulations represent a powerful method for exploringthe conformational space of folded proteins. However, the success has sofar been limited when the method is applied to intrinsically disorderedproteins, a situation that can be attributed to force field inaccuracyand sampling inefficiency. To address the issue, we have developed astrategy to combine the chemical shift information with moleculardynamics simulations for characterizing the structural ensemblescorresponding to intrinsically disordered proteins. This method is basedon the CamShift protocol for calculating the chemical shifts frominter-atomic distances and to calculate forces that minimize thedeviations between experimental and calculated chemical shifts. We haveused chemical shifts as these NMR parameters are most convenient for thestudy of intrinsically disordered proteins, since they, at least inprinciple, contain information about the structure and dynamics of themolecules. To further enhance the sampling efficiency, the method ofmetadynamics approach with replica exchange is added to the protocol.
Project Home
Michele Vendruscolo
Starting Date October 2011


9th European Biophysics Congress, EBSA 2013
July 2013, Lisbon, Portugal

1st Annual meeting of the Centre for Misfolding Diseases
November 2013, Cambridge, UK

Intensive Training Module – Marie Curie Training Network
Protein Structure Analysis using NMR Chemical Shifts
May 2012 - Cambridge, United Kingdom

Complementary Skills Training – Marie Curie Training Network
Self Marketing, Project Management, Benchmarks and Competition in Research
February 2012 - St. Moritz, Switzerland



Scientific Posters:

MD simulations of intrinsically disordered proteins with
replica-averaged chemical shift restraints.
9th European Biophysics Congress, EBSA2013, 13-17 July, Lisbon