Monitoring of seasonal snow cover in Bhutan using remote sensing technique

All major rivers in Bhutan depend on snowmelt for discharge. Therefore, changes in snow cover due to climate change can influence distribution and availability of water. However, information about distribution of seasonal snow cover in Bhutan is not available. The MODIS snow product was used to study snow cover status and trends in Bhutan. Average snow cover area (SCA) of Bhutan estimated for the period 2002 to 2010 was 9030 sq. km, about 25.5% of the total land area. SCA trend of Bhutan for the period 2002-2010 was found to decrease (-3.27 +/- 1.28%). The average SCA for winter was 14,485 sq. km (37.7%), for spring 7411 sq. km (19.3%), for summer 4326 sq. km (11.2%), and for autumn 7788 sq. km (20.2%), mostly distributed in the elevation range 2500-6000 m amsl. Interannual and seasonal SCA trend both showed a decline, although it was not statistically significant for all sub-basins. Pho Chu sub-basin with 19.5% of the total average SCA had the highest average SCA. The rate of increase of SCA for every 100 m elevation was the highest (2.5%) in the Pa Chu sub-basin. The coefficient of variance of 1.27 indicates high variability of SCA in winter.

Interaction Signatures Stabilizing the NAD(P)-Binding Rossmann Fold: A Structure Network Approach

The fidelity of the folding pathways being encoded in the amino acid sequence is met with challenge in instances where proteins with no sequence homology, performing different functions and no apparent evolutionary linkage, adopt a similar fold. The problem stated otherwise is that a limited fold space is available to a repertoire of diverse sequences. The key question is what factors lead to the formation of a fold from diverse sequences. Here, with the NAD(P)-binding Rossmann fold domains as a case study and using the concepts of network theory, we have unveiled the consensus structural features that drive the formation of this fold. We have proposed a graph theoretic formalism to capture the structural details in terms of the conserved atomic interactions in global milieu, and hence extract the essential topological features from diverse sequences. A unified mathematical representation of the different structures together with a judicious concoction of several network parameters enabled us to probe into the structural features driving the adoption of the NAD(P)-binding Rossmann fold. The atomic interactions at key positions seem to be better conserved in proteins, as compared to the residues participating in these interactions. We propose a ``spatial motif'' and several ``fold specific hot spots'' that form the signature structural blueprints of the NAD(P)-binding Rossmann fold domain. Excellent agreement of our data with previous experimental and theoretical studies validates the robustness and validity of the approach. Additionally, comparison of our results with statistical coupling analysis (SCA) provides further support. The methodology proposed here is general and can be applied to similar problems of interest.