Water Quality Index Assessment Of Ground Water In Jakkur Sub Watershed Of Bangalore, Karnataka, India

The water quality index (WQI) is a single number that expresses the quality of water by integrating the water quality variables. The purpose is to provide a simple and concise method for expressing the water quality for different usage. The present work deals with the monitoring of variation of seasonal ground water quality index of ground water for Jakkur sub watershed in Bangalore, Karnataka state of India. For calculating the WQI the following 12 physic-chemical parameters such as pH, Electric Conductivity, Total Dissolved Solids, Total Alkalinity, Chlorides, Total Hardness, Dissolved Oxygen, Fluoride, Calcium, Magnesium, Sulphate and Nitrate have been considered. The water quality index value of ground water was 84.46 in rainy season, 77.14 in winter season and 91.22 in summer season. In the present investigation the quality of water was found to be good in and around Jakkur sub watershed

Statical Analysis of Rainfall for Development of Intensity-Duration-Frequency Curves for Upper Cauvery Karnataka by Log-Normal Distribution

Intensity–duration–frequency (IDF) curves are among the most demandable information in meteorology, hydrology and engineering water resources design, planning, operation, and management works. The IDF Curves accessible are for the most part done by fitting arrangement of yearly greatest precipitation force to parametric dispersions. Intensity-durationfrequency (IDF) curves represent the relationship between storm intensity, storm duration and return period. Environmental change is relied upon to intensify the boundaries in the atmosphere factors. Being prone to harsh climate impacts, it is very crucial to study extreme rainfall-induced flooding for short durations over regions that are rapidly growing. One way to approach the extremes is by the application of the Intensity-Duration-Frequency (IDF) curves. The annual maximum rainfall intensity (AMRI) characteristics are often used to construct these IDF curves that are being used in several infrastructure designs for urban areas. Thus, there is a necessity to obtain high temporal and spatial resolution rainfall information. Many urban areas of developing countries lack long records of short-duration rainfall. The shortest duration obtained is normally at a daily scale/24 h. This paper suggests their generation based on annual daily maximum rainfall (ADMR) records. Rainfall data of 23 (Twenty three) hydrological years of all stations were used. Maximum rainfall frequency analysis was made by LogNormal Distribution method

Structural basis of adenylyl cyclase 9 activation

Adenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Gαs subunit and is autoinhibited by the AC9 C-terminus. Although our recent structural studies of the AC9-Gαs complex provided the framework for understanding AC9 autoinhibition, the conformational changes that AC9 undergoes in response to activator binding remains poorly understood. Here, we present the cryo-EM structures of AC9 in several distinct states: (i) AC9 bound to a nucleotide inhibitor MANT-GTP, (ii) bound to an artificial activator (DARPin C4) and MANT-GTP, (iii) bound to DARPin C4 and a nucleotide analogue ATPαS, (iv) bound to Gαs and MANT-GTP. The artificial activator DARPin C4 partially activates AC9 by binding at a site that overlaps with the Gαs binding site. Together with the previously observed occluded and forskolin-bound conformations, structural comparisons of AC9 in the four conformations described here show that secondary structure rearrangements in the region surrounding the forskolin binding site are essential for AC9 activation

Structural basis of adenylyl cyclase 9 activation

Adenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Gαs subunit and is autoinhibited by the AC9 C-terminus. Although our recent structural studies of the AC9-Gαs complex provided the framework for understanding AC9 autoinhibition, the conformational changes that AC9 undergoes in response to activator binding remains poorly understood. Here, we present the cryo-EM structures of AC9 in several distinct states: (i) AC9 bound to a nucleotide inhibitor MANT-GTP, (ii) bound to an artificial activator (DARPin C4) and MANT-GTP, (iii) bound to DARPin C4 and a nucleotide analogue ATPαS, (iv) bound to Gαs and MANT-GTP. The artificial activator DARPin C4 partially activates AC9 by binding at a site that overlaps with the Gαs binding site. Together with the previously observed occluded and forskolin-bound conformations, structural comparisons of AC9 in the four conformations described here show that secondary structure rearrangements in the region surrounding the forskolin binding site are essential for AC9 activation

Groundwater resource assessment in Kushavathi watershed, Chickballapur district, Karnataka, India

In the present study, an attempt has been made to delineate the groundwater potential zones in the Kushavathi watershed, Chickballapur district, Karnataka. The study has been for targeting groundwater in hard rock terrain by adopting remote sensing and GIS techniques. Information on geomorphology and land use is generated using the remote sensing data. The hydrogeomorphic units like floodplains and valleys have good groundwater potential, and pediplains and pediments have moderate to poor groundwater potential. The structural hills, denudational hills and inselberg are indicated as runoff zones. The weathered and fractured zone constitute the aquifer system in the area

Structural basis of adenylyl cyclase 9 activation

Adenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Gαs subunit and is autoinhibited by the AC9 C-terminus. Although our recent structural studies of the AC9-Gαs complex provided the framework for understanding AC9 autoinhibition, the conformational changes that AC9 undergoes in response to activator binding remains poorly understood. Here, we present the cryo-EM structures of AC9 in several distinct states: (i) AC9 bound to a nucleotide inhibitor MANT-GTP, (ii) bound to an artificial activator (DARPin C4) and MANT-GTP, (iii) bound to DARPin C4 and a nucleotide analogue ATPαS, (iv) bound to Gαs and MANT-GTP. The artificial activator DARPin C4 partially activates AC9 by binding at a site that overlaps with the Gαs binding site. Together with the previously observed occluded and forskolin-bound conformations, structural comparisons of AC9 in the four conformations described here show that secondary structure rearrangements in the region surrounding the forskolin binding site are essential for AC9 activation.ISSN:2041-172