Rigidity and functionalization

Fulop, V., and Jones, D. T. (1999). Beta propellers Structural rigidity and functional diversity. Curr. Opin. Struct. Biol. 9, 715—721. 

Fulop V, Jones DT. Beta propellers structural rigidity and functional diversity. Curr Opin Struct Biol 1999 9(6) 715 721. 

The paper discusses the application of dynamic indentation method and apparatus for the evaluation of viscoelastic properties of polymeric materials. The three-element model of viscoelastic material has been used to calculate the rigidity and the viscosity. Using a measurements of the indentation as a function of a current velocity change on impact with the material under test, the contact force and the displacement diagrams as a function of time are plotted. Experimental results of the testing of polyvinyl chloride cable coating by dynamic indentation method and data of the static tensile test are presented. 

In milk fat, cholesterol is associated with Hpoproteins in the milk fat globule. It is also a component of animal membranes and controls rigidity and permeabihty of the membranes. Cholesterol has interesting surface properties and can occur in Hquid crystalline forms. Plants contain sterols such as P-sitosterol [83-46-5] (4b) or stigmasterol [83-48-7] (4c). Their functions in plant metaboHsm are not yet well understood. Analysis of sterols has proven useful for detection of adulteration of edible fats (9). 

Figure 8 Effects of spin diffusion. The NOE between two protons (indicated by the solid line) may be altered by the presence of alternative pathways for the magnetization (dashed lines). The size of the NOE can be calculated for a structure from the experimental mixing time, and the complete relaxation matrix, (Ry), which is a function of all mterproton distances d j and functions describing the motion of the protons, y is the gyromagnetic ratio of the proton, ti is the Planck constant, t is the rotational correlation time, and O) is the Larmor frequency of the proton m the magnetic field. The expression for (Rjj) is an approximation assuming an internally rigid molecule.

The secondary structure elements, formed in this way and held together by the hydrophobic core, provide a rigid and stable framework. They exhibit relatively little flexibility with respect to each other, and they are the best-defined parts of protein structures determined by both x-ray and NMR techniques. Functional groups of the protein are attached to this framework, either directly by their side chains or, more frequently, in loop regions that connect sequentially adjacent secondary structure elements. We will now have a closer look at these structural elements. 

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