By Peter Tompa
"The publication is simply terrific- an intensive, entire and lucid dialogue of intrinsically disordered proteins" --Joel L. Sussman, Weizmann Institute of Science
"Tompa's masterly compendium on Intrinsically Disordered Proteins arrives at simply the ideal time to fill a conspicuous void in this very important subject. His eminently readable e-book is wide adequate to teach rookies yet deep adequate to notify experts." -George Rose, Ph.D., Johns Hopkins college
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Additional resources for Structure and Function of Intrinsically Disordered Proteins
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Copyright by Elsevier. preventing its inappropriate interactions potentially leading to aggregation, and facilitating the assembly of multi-subunit proteins (Csermely 1999; Ellis 2006). Many chaperones have been first described as heat shock proteins (Hsps), because their expression is stimulated by stress conditions such as elevated temperatures. 1). These chaperones use ATP energy in their action. 7 Unfolding of a protein: lessons from polymer theory The interest in describing the unfolded/denatured state of proteins has been motivated by the fact that it serves as a reference point for understanding both thermodynamic and mechanistic aspects of folding.
Underlying these definitions is the idea that a domain is a functional unit of the protein that carries a distinct function on its own (Vogel et al. 2004). An additional and often underappreciated level of structural complexity stems from the fact that proteins are not static, but rather undergo constant motions. , conformational changes that often form part of the function). The atomic vibrations are very fast, occurring on the order of picoseconds, whereas conformational changes may be much slower, taking seconds or even longer.
Such mutations play a basic role in evolution by generating variants of the protein. 2 Local structure and dihedral angle around the α-carbon in a polypeptide chain. A useful descriptor of local conformation of a polypeptide chain is the pair of dihedral angles of the rotation of two planar peptide bonds around the alpha carbon. The example shown is an Ala3 tripeptide: The four atoms of the peptide bonds on either side of Cα are found within a plane, the position of which is described by two torsion angles, Φ (defined as C′-N-Cα-C′) and Ψ (defined as N-Cα-C′-N).