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than ten thousand unique structures of soluble prote<strong>in</strong>s only few of them have been studied at atomic resolution/level. The complete<br />

understand<strong>in</strong>g of the structure and function of membranous prote<strong>in</strong>s is crucial for design<strong>in</strong>g better therapeutical molecules.<br />

Plasma membrane: A complex lipid-prote<strong>in</strong> compound<br />

Plasma membrane consists of lipids with highest percentage (60-70%) followed by the prote<strong>in</strong> with lesser <strong>in</strong> percentage (30-40%). In<br />

a few percentage cholesterol and other molecules are also present <strong>in</strong> plasma membrane. In the complex structure of plasma membrane<br />

the mobility and diffusion of prote<strong>in</strong> become irregular with respect to diffusion coefficient and show<strong>in</strong>g lower value as compared to<br />

the artificial membrane systems. Probably, all this happens due to <strong>in</strong>teraction of prote<strong>in</strong> molecules with other molecules, cytoskeleton<br />

<strong>in</strong>teraction and presence of sterol and sph<strong>in</strong>golipid enriched doma<strong>in</strong>s known as lipid rafts [3-7].<br />

Figure 5: Prote<strong>in</strong> Diffusion <strong>in</strong> Cell is affected by Multiple Biological Processes.<br />

Particularly three techniques are used for analyz<strong>in</strong>g dynamics <strong>in</strong> prote<strong>in</strong>s <strong>in</strong>clud<strong>in</strong>g fluorescence recovery after photo bleach<strong>in</strong>g,<br />

fluorescence correlation spectroscopy and s<strong>in</strong>gle particle track<strong>in</strong>g. Moreover, physical models are engaged <strong>in</strong> analyz<strong>in</strong>g the data for<br />

prote<strong>in</strong> dynamics that represents extraord<strong>in</strong>ary features of the biophysical nature regard<strong>in</strong>g prote<strong>in</strong> dynamics and membrane doma<strong>in</strong>s<br />

<strong>in</strong> membranes. Up till now, there rema<strong>in</strong> considerable unknown <strong>in</strong>formation among cholesterol dependent lipid micro-doma<strong>in</strong>s, prote<strong>in</strong><br />

<strong>in</strong>teractions, and cause of the underly<strong>in</strong>g cytoskeleton. Innovative techniques of microscopy may provide better sequential and spatial<br />

resolution ensu<strong>in</strong>g <strong>in</strong> more perfect identification and recognition of prote<strong>in</strong>s as well as its dynamics <strong>in</strong> biological system. The k<strong>in</strong>etic<br />

aspects of prote<strong>in</strong> <strong>in</strong> a membrane and the types of motion that it conta<strong>in</strong> go through by the lateral organization of cellular boundary. Fluid<br />

mosaic model given by S<strong>in</strong>ger and Nicolson projected that the cell membrane conta<strong>in</strong>s membrane-associated prote<strong>in</strong>s which can diffuse<br />

(spread) liberally with Brownian movement [8] and randomly distributed on the cellular surface.<br />

Importance of Dynamics <strong>in</strong> Prote<strong>in</strong>s<br />

The dynamic behavior of prote<strong>in</strong>s is dist<strong>in</strong>guished to play significant role <strong>in</strong> prote<strong>in</strong> function. Diverse characteristics of prote<strong>in</strong><br />

function are <strong>in</strong>fluenced by dynamics of prote<strong>in</strong>. For example, prote<strong>in</strong> to prote<strong>in</strong> identification [9], prote<strong>in</strong>-DNA associations [10] and<br />

enzyme-substrate bond<strong>in</strong>g and activity of enzymes [11-13] are all resolute by the structural flexibility of the prote<strong>in</strong> molecule and side<br />

cha<strong>in</strong>s, result<strong>in</strong>g <strong>in</strong>to characteriz<strong>in</strong>g not only the structure, but also dynamic properties as well. On a wide variety of time scales, the<br />

dynamics of prote<strong>in</strong>s are thoroughly related to function of prote<strong>in</strong>. Fast as well as moderately fast fluctuations of prote<strong>in</strong> structure<br />

facilitate a prote<strong>in</strong> to sample a complex conformational-energy landscape. Such motions of atoms or residues give rise to the slower<br />

processes associated with prote<strong>in</strong> function. Molecular dynamics (MD) simulations have shown that a prote<strong>in</strong> can sample thousands of<br />

conformations with<strong>in</strong> a very short time. Determ<strong>in</strong>ation of prote<strong>in</strong> dynamics by X-ray, NMR and other experimental techniques and<br />

theory helped <strong>in</strong> understand<strong>in</strong>g the dynamics that provides an important connection between prote<strong>in</strong> function and prote<strong>in</strong> structure [14].<br />

Dynamics of prote<strong>in</strong>s and mRNA<br />

mRNA and prote<strong>in</strong> molecules are dynamic entities, and their presence <strong>in</strong> the cell is the outcome of contrast<strong>in</strong>g processes that br<strong>in</strong>g<br />

about their biosynthesis or destruction. The abundance-weighted total of all prote<strong>in</strong>s <strong>in</strong> a cell or sub-cellular space is also dynamic.<br />

The amount of a true <strong>in</strong>tracellular prote<strong>in</strong> <strong>in</strong> a cell is the result of the oppos<strong>in</strong>g processes of prote<strong>in</strong> synthesis and prote<strong>in</strong> degradation.<br />

However, for extracellular prote<strong>in</strong>s, it has to factor <strong>in</strong> the irreversible loss due to secretion. If a prote<strong>in</strong> decreases <strong>in</strong> amount <strong>in</strong> a cell, this<br />

can be a consequence of a reduction of mRNA, or of a decrease <strong>in</strong> ribosomal activity or translation <strong>in</strong>itiation. Equally possible it could be<br />

the consequence of enhanced degradation of the prote<strong>in</strong>.<br />

Prote<strong>in</strong> Motions<br />

Prote<strong>in</strong>s are composed of multiple doma<strong>in</strong>s, whose flexibility and mobility lead to a great deal of versatility <strong>in</strong> their function. Prote<strong>in</strong><br />

dynamics, at the doma<strong>in</strong> level, is a controll<strong>in</strong>g <strong>in</strong>fluence <strong>in</strong> the allosteric formation of prote<strong>in</strong> complexes, <strong>in</strong> catalysis, <strong>in</strong> cell signal<strong>in</strong>g and<br />

regulation, <strong>in</strong> cellular locomotion and <strong>in</strong> metabolic transport.<br />

OMICS Group eBooks<br />

007

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