Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Rifat Nawaz"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Abstract Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the p
Externí odkaz:
https://doaj.org/article/eb709fb6a7a34864b0ace9527010abca
Akademický článek
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Publikováno v:
2022 IEEE 46th Annual Computers, Software, and Applications Conference (COMPSAC).
Publikováno v:
Bioinformation
Salt-bridges (sb) play an important role in the folding and stability of proteins. This is deduced from the evaluation of net energy in the microenvironments (ME, residues that are 4Å away from positive and negative partners of salt-bridge and inter
Screening and molecular characterization of lethal mutations of human homogentisate 1, 2 dioxigenase
Autor:
Amal Kumar Bandyopadhyay, Sahini Banerjee, Arnab Nayek, Parth Sarthi Sen Gupta, Rifat Nawaz Ui Islam, Malay Kumar Rana
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 39:1661-1671
Alkaptonuria (AKU) is an autosomal recessive disorder, which is caused by a site-specific mutation(s) and thus, impaired the function of Homogentisate-1, 2-dioxygenase (HGD), an essential enzyme for the catabolism of phenylalanine and tyrosine. Among
Autor:
Debanjan Mitra, Amal Kumar Bandyopadhyay, Arunava Goswami, Saba Yasmeen, Sahini Banerjee, Rifat Nawaz Ul Islam
Publikováno v:
Bioinformation. 15:95-103
Halophilic proteins have greater abundance of acidic over basic residues in sequence. In structure, the surface is decorated by negative charges, with lower content of Lysine. Using sequence BLOCKs and 3D model of malate dehydrogenase from halophilic
Autor:
Arunava Goswami, Rifat Nawaz Ul Islam, Debanjan Mitra, Amal Kumar Bandyopadhyay, Sahini Banerjee
Publikováno v:
Bioinformation
We analyzed the water-ferredoxin interaction in mesophilic (moderate temperature) algae (PDB ID: 1AWD) and halophilic (salt-tolerant) archaea (PDB ID: 1DOI) using POWAIND version 2.0 (a protein-water interactions calculation program). It is found tha
Autor:
Arunava Goswami, Debanjan Mitra, Amal Kumar Bandyopadhyay, Rifat Nawaz Ul Islam, Sahini Banerjee
Publikováno v:
Bioinformation
Thermophilic proteins function at high temperature, unlike mesophilic proteins. Thermo-stability of these proteins is due to the unique buried and networked salt-bridge (BNSB). However, it is known that the desolvation cost of BNSB is too high compar
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
Akademický článek
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