Revisiting the Myths of Protein Interior: Studying Proteins with Mass-Fractal Hydrophobicity-Fractal and Polarizability-Fractal Dimensions

A robust marker to describe mass, hydrophobicity and polarizability distribution holds the key to deciphering structural and folding constraints within proteins. Since each of these distributions is inhomogeneous in nature, the construct should be sensitive in describing the patterns therein. We show, for the first time, that the hydrophobicity and polarizability distributions in protein interior follow fractal scaling. It is found that (barring ‘all-α’) all the major structural classes of proteins have an amount of unused hydrophobicity left in them. This amount of untapped hydrophobicity is observed to be greater in thermophilic proteins, than that in their (structurally aligned) mesophilic counterparts. ‘All-β’(thermophilic, mesophilic alike) proteins are found to have maximum amount of unused hydrophobicity, while ‘all-α’ proteins have been found to have minimum polarizability. A non-trivial dependency is observed between dielectric constant and hydrophobicity distributions within (α+β) and ‘all-α’ proteins, whereas absolutely no dependency is found between them in the ‘all-β’ class. This study proves that proteins are not as optimally packed as they are supposed to be. It is also proved that origin of α-helices are possibly not hydrophobic but electrostatic; whereas β-sheets are predominantly hydrophobic in nature. Significance of this study lies in protein engineering studies; because it quantifies the extent of packing that ensures protein functionality. It shows that myths regarding protein interior organization might obfuscate our knowledge of actual reality. However, if the later is studied with a robust marker of strong mathematical basis, unknown correlations can still be unearthed; which help us to understand the nature of hydrophobicity, causality behind protein folding, and the importance of anisotropic electrostatics in stabilizing a highly complex structure named ‘proteins’

Where do the platelets go? A simulation study of fully resolved blood flow through aneurysmal vessels

Despite the importance of platelets in the formation of a thrombus, their transport in complex flows has not yet been studied in detail. In this paper we simulated red blood cells and platelets to explore their transport behaviour in aneurysmal geometries. We considered two aneurysms with different aspect ratios (AR = 1.0, 2.0) in the presence of fast and slow blood flows (Re = 10, 100), and examined the distributions of the cells. Low velocities in the parent vessel resulted in a large stagnation zone inside the cavity, leaving the initial distribution almost unchanged. In fast flows, an influx of platelets into the aneurysm was observed, leading to an elevated concentration. The connection of the platelet-rich cell-free layer (CFL) with the outer regions of the recirculation zones leads to their increased platelet concentration. These platelet-enhanced recirculation zones produced a diverse distribution of cells inside the aneurysm, for the different aspect ratios. A thin red blood CFL that was occupied by platelets was observed on the top of the wide-necked aneurysm, whereas a high-haematocrit region very close to the vessel wall was present in the narrow-necked case. The simulations revealed that non-trivial distributions of red blood cells and platelets are possible inside aneurysmal geometries, giving rise to several hypotheses on the formation of a thrombus, as well as to the wall weakening and the possible rupture of an aneurysm