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BioEssays 8/2010
Author(s) -
CaetanoAnollés Gustavo,
Mittenthal Jay
Publication year - 2010
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201090031
Subject(s) - protein data bank (rcsb pdb) , sequence (biology) , folding (dsp implementation) , diagram , stability (learning theory) , cytochrome , bundle , grid , protein folding , function (biology) , crystallography , protein structure , biology , dimension (graph theory) , computational biology , physics , evolutionary biology , computer science , chemistry , genetics , combinatorics , geometry , mathematics , materials science , biochemistry , engineering , database , machine learning , electrical engineering , composite material , enzyme
Cover Photograph: The interplay of protein stability and function in sequence space , as discussed by Gustavo Caetano‐Anollés and Jay Mittenthal on pages 655–658 of this issue. The grid diagram depicts a multidimensional sequence space (flattened into a two‐dimensional view) of protein sequences that change into others by single‐point mutations (the third dimension represents thermodynamic stability). All proteins in the grid fold into a same three‐dimensional (3D) structure, a four‐helix bundle structure typical of cytochrome cb562 (a metalloprotein used to study metal‐induced protein stability and homodimerization; PDB entry 3L1M). In the diagram, cytochrome proteins drift in evolution along the grid (colored regions) while folding into the same 3D structure and while searching for increases in protein stability (i.e. dents in the grid). This results in sections of the proteins that are evolutionarily conserved due to constraints imposed by the interplay of stability and function (grey regions close to metal‐binding sites in the bundles). Image and concept developed by Derek Caetano‐Anollés.