Exploring the range of protein flexibility, from a structural proteomics perspective.
Changes in protein conformation play a vital role in biochemical processes, from biopolymer synthesis to membrane transport. Initial systematizations of protein flexibility, in a database framework, concentrated on the movement of domains and linkers. Movements were described in terms of simple sliding and hinging mechanisms of individual secondary structural elements. Recently, the accelerated pace and sophistication of methods for structural characterization of proteins has allowed high-resolution studies of increasingly complex assemblies and conformational changes. New data emphasize a breadth of possible structural mechanisms, particularly the ability to drastically alter protein architecture and the native flexibility of many structures.
Gerstein
Mark
M
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Ave, New Haven, CT 06520, USA. mark.gerstein@yale.edu
Echols
Nathaniel
N
D018583:Pliability; D040081:Protein Array Analysis; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D040901:Proteomics
D011506:Proteins