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1.
Indian J Ophthalmol ; 2019 Aug; 67(8): 1332-1333
Article | IMSEAR | ID: sea-197433
2.
Article in English | IMSEAR | ID: sea-114002

ABSTRACT

The present study aims at the assessment of groundwater quality in and around the Vrishabhavathi Valley, the erstwhile fresh water stream, today carrying huge quantities of industrial, agricultural and domestic effluents from the western part of Bangalore metropolis. Groundwater samples were collected from both bore wells and open wells along the Vrishabhavathi watershed and subjected to a comprehensive physico-chemical and bacteriological analysis. The study revealed that 57% of the samples were non-potable due to their values when compared to the BIS standards. The concentrations of nitrate and total hardness were found higher than the standards in 43.33% and 40% of the samples respectively. 50% of the samples examined, indicated bacterial contamination in the groundwater.


Subject(s)
Electric Conductivity , Environmental Monitoring , Fresh Water/chemistry , Hydrogen-Ion Concentration , India , Nitrates/analysis , Water Pollutants, Chemical/analysis , Water Supply
3.
J Biosci ; 2007 Jun; 32(4): 693-704
Article in English | IMSEAR | ID: sea-110974

ABSTRACT

Ion pairs contribute to several functions including the activity of catalytic triads, fusion of viral membranes, stability in thermophilic proteins and solvent-protein interactions. Furthermore, they have the ability to affect the stability of protein structures and are also a part of the forces that act to hold monomers together. This paper deals with the possible ion pair combinations and networks in 25% and 90% non-redundant protein chains. Different types of ion pairs present in various secondary structural elements are analysed. The ion pairs existing between different subunits of multisubunit protein structures are also computed and the results of various analyses are presented in detail. The protein structures used in the analysis are solved using X-ray crystallography, whose resolution is better than or equal to 1.5 A and R-factor better than or equal to 20%. This study can, therefore, be useful for analyses of many protein functions. It also provides insights into the better understanding of the architecture of protein structure.


Subject(s)
Crystallography, X-Ray , Ions , Models, Molecular , Protein Conformation , Proteins/chemistry
4.
J Indian Soc Pedod Prev Dent ; 1984 Mar; 2(1): 32-3
Article in English | IMSEAR | ID: sea-114984
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