The Protein Chart

What the Periodic Table did for the visualization of chemical concepts, this chart will achieve for structural biology. This truly innovative product addresses a growing need in the scientific community –– making the entire spectrum of protein structures instantly accessible on one handy chart. By way of a clever arrangement into rows and columns, this is much more than a simple field guide to individual protein structures: It is also an invaluable aid to understanding the principles behind protein structure diversity.
There is simply no better tool to introduce students to the secrets of proteins.

Spis treści:
INSIDE FACING
The main table displays 86 stuctural domains, organized into four major (alpha proteins, beta proteins, alpha/beta proteins, knots and fibers) and 26 minor architectural classes (such as sandwich, barrel, horseshoe, orthogonal bundle etc.).
For each domain, a representative structure is shown alongside structural and functional information for the fold group.
The abundance of each fold group in the currently sequenced more than 500 genomes is given, with the 10 most abundant "superfolds" highlighted.
OUTSIDE FACING
A satellite table of oligomeric proteins depicts 37 oligomer architectures, ordered according to their highest order rotation axis. For each class, a representative structure is displayed, along with structural and functional information on the class.
Also on the chart is a summary of 10 basic secondary structure topologies (shown in a 2D representation) and of the 12 most important three–dimensional structural motifs such as HTH, EF hand, HLH, Zn finger, P–loop, Greek key etc.


Nota biograficzna:
Richard Garratt studied Biochemistry at the University of London (UK), receiving a PhD in protein crystallography from Birkebeck College, London, in 1989. He then moved to the University of Sao Paulo (Brasil), where he was appointed Professor in 1996. Pro fessor Garratt heads the crystallography group at the San Carlos Institute of Physics, focusing his research on protein structure determination and rational drug design. He is also the inventor of a widely acclaimed protein structure modeling kit for educational purposes.
Christine Orengo studied Physics at the Universities of Bristol and Aberdeen (UK), receiving a PhD in Biochemistry from University College, London in 1984. She then became a MRC fellow and was later appointed Professor of Bioinformatics at University College. Together with Janet Thornton, Professor Orengo has developed the CATH protein structure database that is widely used to compare and identify evolutionarily related proteins.