Properties of globular proteins

Haynes CA, Sliwinski E, Norde W (1994) Structural and electrostatic properties of globular proteins at a polystyrene-water interface. J Colloid Interf Sci 164 394 109... 

Real proteins are built up both from hydrophobic and polar amino acid residues, some of the latter can be charged. Many of the conformational and collective properties of proteins are due to a complex interplay between short-range (hydrophobic) effects and long-range (Coulomb) interactions. Electrostatic effects can also determine some of the unique solution properties of globular proteins. We have already discussed the results of simulations... 

An increasing number of investigators have recently come to believe that the following generalized scheme of interactions accounts for the properties of globular protein and DNA molecules in aqueous solutions. From results such as have been discussed in previous sections, and from a considerable amount of other kinds of evidence (Kauzmann, 1959), it is con-... 

Optical Rotatory Properties of Globular Proteins with Native Xe Values Grealer Than 30 mu ... 

Richardson, R K. and Ross-Murphy, S. B. 1981a. Mechanical properties of globular protein gels ... 

Fractal Interpretation Consistent with Known Properties of Globular Proteins... 

Garcia de la Torre, J., Huertas, M.L., Carrasco, B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 2000, 78, 719-30. 

One can see that the HP heteropolymer obtained as a result of the simple one-step coloring procedure can self-assemble into a segregated core-shell microstructure, thus resembling some of the basic properties of globular proteins. The core of protein-like globule is much more compact and better formed as compared to that observed for RCPs it is surrounded by the loops of hydrophilic segments, which stabilize the core. 

DLS is an established technique for protein characterization. For example, to And optimum protein crystalhzation conditions, DLS is used as a prescreening tool to identify critical parameters of the process such as the hydrodynamic size, polydispersity, and aggregation factors. DLS is also used as a method to characterize the hydrodynamic properties of globular proteins in electrolyte solutions. However, applications of DLS to characterize charged protein solutions, just as any other charged molecules in solution, could face certain difficulties in subsequent data treatment. 

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