The Protein Chart
1. Auflage November 2007
6 Seiten, Nonbook
Is it possible to represent the whole world of protein structures in one handy table? Take a look at this chart and see for yourself. Intuitive and stimulating, this ingenious 'Periodic Table' is an invaluable aid to understanding the principles behind protein structure diversity
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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.
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.
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.
(Donald Voet, author of the textbooks "Biochemistry" and "Fundamentals of Biochemistry")
"The ideal tool to understand and to teach the principles of protein structure, and beautifully designed. I wholeheartedly recommend it."
(Robert Huber, Winner of the 1988 Nobel Prize in Chemistry)
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.