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pro vyhledávání: '"Buddhadev Mondal"'
Autor:
Arnab Nayek, Parth Sarthi Sen Gupta, Shyamashree Banerjee, Buddhadev Mondal, Amal K Bandyopadhyay
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93862 (2014)
Halophilic proteins have greater abundance of acidic over basic and very low bulky hydrophobic residues. Classical electrostatic stabilization was suggested as the key determinant for halophilic adaptation of protein. However, contribution of specifi
Externí odkaz:
https://doaj.org/article/e8a48a808d2142f6832b7481e9b2fef9
Publikováno v:
INTERNATIONAL JOURNAL OF SCIENTIFIC RESEARCH. :35-39
AIMS: During COVID-19 pandemic, health care resources are being diverted towards the acute crisis, de-emphasizing the routine medical care. It is not only less access of health care but people also avoiding health care facilities during this pandemic
Autor:
Sovan Samanta, Sk Nazibar Rahaman, Surajit Das, Biplab Giri, Sandeep Kumar Dash, Buddhadev Mondal, Jhimli Banerjee, Kazi Monjur Ali
Publikováno v:
Bangladesh Journal of Medical Science. 20:707-713
Fisheries sector is considered as fast-growing sector in India. At present fish production has increased over time, but it doesn’t change the economic conditions of the fishing community. Fisheries’ daily income is very low and varied depending u
Autor:
Buddhadev Mondal, AmalKumar Bandyopadhyay, Sahini Banerjee, Rifat Nawaz Ul Islam, Parth Sarthi Sen Gupta, Debanjan Mitra
Publikováno v:
Bioinformation
Protein is the most exposed biomolecule in the aqueous environment of the cell. Its structure maintains a delicate balance between the rigidity and the flexibility that imparts binding specificity to its substrate/ligand, etc. Intramolecular interact
Autor:
Buddhadev Mondal, Sahini Banerjee, Sen Gupta Ps, Mitra D, Ul Islam Rn, Amal Kumar Bandyopadhyay
Publikováno v:
Bioinformation
Global minimal structure of protein/enzyme is energetically compromised that maintains an intricate balance between the rigidity and the flexibility. Such a state makes it interactive to its ligand molecules. Although protein data bank files (PDB) ma
Autor:
Amal Kumar Bandyopadhyay, Buddhadev Mondal, Rifat Nawaz Ul Islam, Sudipta Mondal, Shyamashree Banerjee, Parth Sarthi Sen Gupta
Publikováno v:
Bioinformation
Salt-bridge and network salt-bridge are specific electrostatic interactions that contribute to the overall stability of proteins. In hierarchical protein folding model, these interactions play crucial role in nucleation process. The advent and growth
Autor:
Buddhadev Mondal, Arnab Nayek, Shyamashree Banerjee, Amal Kumar Bandyopadhyay, Parth Sarthi Sen Gupta
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 4, p e93862 (2014)
PLoS ONE, Vol 9, Iss 4, p e93862 (2014)
Halophilic proteins have greater abundance of acidic over basic and very low bulky hydrophobic residues. Classical electrostatic stabilization was suggested as the key determinant for halophilic adaptation of protein. However, contribution of specifi
Autor:
Rifat Nawaz Ul Islam, Parth Sarthi Sen Gupta, Amal Kumar Bandyopadhyay, Sudipta Mondal, Buddhadev Mondal, Shyamashree Banerjee
Publikováno v:
Bioinformation
In the genomic and proteomic era, efficient and automated analyses of sequence properties of protein have become an important task in bioinformatics. There are general public licensed (GPL) software tools to perform a part of the job. However, comput