Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Rifat Nawaz Ul Islam"'
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
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
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
Autor:
P.K.D. Mohapatra, Shyamashree Banerjee, S. Yasmeen, Debanjan Mitra, Amal Kumar Bandyopadhyay, Rifat Nawaz Ul Islam
Publikováno v:
Biotechnology and Biological Sciences ISBN: 9781003001614
Biotechnology and Biological Sciences
Biotechnology and Biological Sciences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9400cab9cc899579e5a2f82918f837fd
https://doi.org/10.1201/9781003001614-18
https://doi.org/10.1201/9781003001614-18
Autor:
Chittran Roy, S. Yasmeen, Debanjan Mitra, Amal Kumar Bandyopadhyay, Rifat Nawaz Ul Islam, Sahini Banerjee
Publikováno v:
Biotechnology and Biological Sciences ISBN: 9781003001614
Biotechnology and Biological Sciences
Biotechnology and Biological Sciences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dacc4a95628657211e94b575cca0ffac
https://doi.org/10.1201/9781003001614-25
https://doi.org/10.1201/9781003001614-25
Autor:
Sahini Banerjee, Sudip Bhattacharyya, Inul Ansary, Arunava Goswami, S. Yasmeen, Debanjan Mitra, Amal Kumar Bandyopadhyay, Rifat Nawaz Ul Islam
Publikováno v:
Biotechnology and Biological Sciences ISBN: 9781003001614
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4158bd5a59b7e7807ace29dbd72cac58
https://doi.org/10.1201/9781003001614-24
https://doi.org/10.1201/9781003001614-24
Autor:
Amal Kumar Bandyopadhyay, Rifat Nawaz Ul Islam, Parth Sarthi Sen Gupta, Vishma Pratap Sur, Shyamashree Banerjee
Publikováno v:
Bioinformation
Orthologous proteins, form due to divergence of parental sequence, perform similar function under different environmental and biological conditions. Amino acid changes at locus specific positions form hetero-pairs whose role in BLOCK evolution is yet