Proteins: Structure, Function, and Engineering by Alexei V. Finkelstein, Alexander M. Gutin (auth.), B. B.

By Alexei V. Finkelstein, Alexander M. Gutin (auth.), B. B. Biswas, Siddhartha Roy (eds.)

Here, researchers assessment the most recent breakthroughs in protein examine. Their contributions discover rising rules and methods and survey very important periods of proteins that might play key roles within the field's destiny. Articles research the opportunity of a Boltzman-like distribution in protein substructures, the hot means of Raman spectroscopy, and compact intermediate states of protein folding. This well-illustrated quantity additionally gains insurance of proteins that bind nucleic acids.

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Extra resources for Proteins: Structure, Function, and Engineering

Example text

It is clear that for many proteins most denaturing conditions do not lead to a fully unfolded protein (random coil), but rather to species with substantial secondary structure and substantial compactness, relative to the fully unfolded state. , a minimum in the free energy profile for the reaction), and compact substates of the unfolded state (Palleros et al.. 1993). It is important to note that it is often experimentally difficult to distinguish between these two types of compact denatured states, especially by spectral methods.

Mv. Protein Chem. 23:121-218. Thornton, J. , Flores, T. , Jones, D. , and Swindells, M. , 1991, Prediction of progress at last, Nature 354:105-106. Udgaonkar, J. , and Baldwin, R. , 1990, Early folding intermediate of ribonuclease A, Proc. Natl. Acad. Sci. USA 87:8197-8201. Watson, H. , 1969, The stereochemistry of the protein myoglobin, Prog. Stereochem. 4:299-333. Zimm, B. , and Bragg, J. , 1959, Theory of the phase transition between helix and random coil in polypeptide chains, J. Chem. Phys.

Recent investigations have now made it clear that for both intermediates and unfolded states the degree of folding and compactness can vary over a wide range depending on the experimental conditions. A particularly good example of this is the Escherichia coli molecular chaperone DnaK. , 1993). Similarly, the unfolded state, when first detected at relatively low denaturant concentration, has Rs = 53 A, whereas at concentrations of guanidine HCI above 4 M its Rs is 69 A.. The compact intermediate is sufficiently stable and sufficiently well separated in terms of energy barriers from the native and unfolded states that it is readily observed under equilibrium conditions by size-exclusion high-pressure liquid chromatography (HPLC).

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