Maximum magnitude estimation considering the regional rupture character

The main objective of the paper is to develop a new method to estimate the maximum magnitude (M (max)) considering the regional rupture character. The proposed method has been explained in detail and examined for both intraplate and active regions. Seismotectonic data has been collected for both the regions, and seismic study area (SSA) map was generated for radii of 150, 300, and 500 km. The regional rupture character was established by considering percentage fault rupture (PFR), which is the ratio of subsurface rupture length (RLD) to total fault length (TFL). PFR is used to arrive RLD and is further used for the estimation of maximum magnitude for each seismic source. Maximum magnitude for both the regions was estimated and compared with the existing methods for determining M (max) values. The proposed method gives similar M (max) value irrespective of SSA radius and seismicity. Further seismicity parameters such as magnitude of completeness (M (c) ), ``a'' and ``aEuro parts per thousand b `` parameters and maximum observed magnitude (M (max) (obs) ) were determined for each SSA and used to estimate M (max) by considering all the existing methods. It is observed from the study that existing deterministic and probabilistic M (max) estimation methods are sensitive to SSA radius, M (c) , a and b parameters and M (max) (obs) values. However, M (max) determined from the proposed method is a function of rupture character instead of the seismicity parameters. It was also observed that intraplate region has less PFR when compared to active seismic region.

Generating artificial homologous proteins according to the representative family character in molecular mechanics properties - an attempt in validating an underlying rule of protein evolution

The molecular mechanics property is the foundation of many characters of proteins. Based on intramolecular hydrophobic force network, the representative family character underlying a protein’s mechanics property is described by a simple two-letter scheme. The tendency of a sequence to become a member of a protein family is scored according to this mathematical representation. Remote homologs of the WW-domain family could be easily designed using such a mechanistic signature of protein homology. Experimental validation showed that nearly all artificial homologs have the representative folding and bioactivity of their assigned family. Since the molecular mechanics property is the only consideration in this study, the results indicate its possible role in the generation of new members of a protein family during evolution.