By Peter Tompa
"The publication is simply tremendous- a radical, finished 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 best time to fill a conspicuous void in this very important subject. His eminently readable booklet is huge adequate to teach newcomers yet deep sufficient to notify experts." -George Rose, Ph.D., Johns Hopkins college
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Extra info for Structure and Function of Intrinsically Disordered Proteins
For example, alcohol dehydrogeanse is a symmetric dimer of two identical subunits. Hemoglobin, on the other hand, is composed as a dimer of dimers of two different subunits and has a structure α2β2. More complex cases are tubulin, which is an αβ dimeric protein that polymerizes to form microtubules (αβ)n, and the closed structure of the coat of tomato bushy stunt virus composed of 180 subunits (Garrett and Grisham 2007). 6 Folding of a protein In his seminal experiments, Anfinsen has shown that the folded state of a protein does not depend on the initial conditions of denaturation (Anfinsen 1973).
The folded structure is highly ordered; thus –TΔSchain is a large positive quantity in the equation. The other terms depend on the nature of amino acid residues in the chain. Apolar groups can better interact with water than with each other; thus ΔHchain is somewhat favorable to the unfolded state. On the other hand, ΔHsolvent is slightly favorable for the folded state, because water molecules can better interact with other water molecules than with exposed apolar side chains. The critical component of the equation, –TΔSsolvent, is large and negative in the presence of apolar groups and strongly favors the folded state, because interaction with apolar groups forces water molecules to become ordered.
When it is removed from its native environment in the myelin membrane . . ” Currently, a better definition of disorder is not available. Still, people were reluctant to take notice, although some protein segments with no discernible electron density were already recognized as essential for function (Alber et al. 1983; Bode, Schwager, and Huber 1978; Spolar and Record 1994). Another protein that resisted crystallization for a long time is microtubule-associated protein 2 (MAP2), which also represents an example of the early observation of protein disorder (Hernandez, Avila, and Andreu 1986).