PFF – an integrated database of residues and fragments critical for protein folding


Background Despite decades of work, understanding how proteins fold remains a major research challenge. The fruits of this massive research effort have been: development of (i) methods for predicting the likely structures that protein sequences will adopt, or for simulating the folding process itself; and (ii) databases of structural information (e.g., containing 3D coordinates, fold classifications, structure summary data, and so on). As part of the ongoing endeavour to understand the principles of protein folding, we have been involved in the development of a new, integrated structure information resource, based on a small subset of the PDB [1]. The resource contains information derived from a combination of sequence analysis tools, structure analysis software and fold simulation algorithms; to make the contents more accessible to the wider community, we have also developed a user-friendly frontend for visualising the integrated data. The motivation for combining data from these various approaches is to offer insights into the role of particular types of residues and fragments in protein folding, and hence to improve our understanding of factors that are critical to the folding process in general.

DOI: 10.1186/1752-0509-1-S1-P48

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@article{Corpas2007PFFA, title={PFF – an integrated database of residues and fragments critical for protein folding}, author={Manuel Corpas and James Sinnott and Dave Thorne and Steve Pettifer and Terri K. Attwood and et al.}, journal={BMC Systems Biology}, year={2007}, volume={1}, pages={1-2} }