Zobrazeno 1 - 10
of 165
pro vyhledávání: '"SANJOY BANDYOPADHYAY"'
Autor:
PRITI PRIYADARSHNI, R N PADARIA, R R BURMAN, RASHMI SINGH, SANJOY BANDYOPADHYAY, PRAMOD KUMAR, ARPAN BHOWMIK, ROMEN SHARMA
Publikováno v:
The Indian Journal of Agricultural Sciences, Vol 92, Iss 1 (2022)
Community engagement is a crucial element for effective management of natural resources. This study is aimed at determining the factors and analyzing their path for collective action behavior of farmers towards natural resource management. Two cases
Externí odkaz:
https://doaj.org/article/eb92d5f446ed4f5193e490965f7b3d73
Publikováno v:
Journal of Chemical Information and Modeling. 63:1542-1555
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ff68e261044779d7ad6f7bb1bed474a
https://doi.org/10.1021/acs.jcim.2c01540
https://doi.org/10.1021/acs.jcim.2c01540
Impact of an Ionic Liquid on Amino Acid Side Chains: A Perspective from Molecular Simulation Studies
Publikováno v:
Journal of Chemical Information and Modeling. 63:959-972
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2681248f88f06b62d966d38bf45801c
https://doi.org/10.1021/acs.jcim.2c01310
https://doi.org/10.1021/acs.jcim.2c01310
Publikováno v:
The Journal of Physical Chemistry B. 127:121-132
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ebda378ebd0ab0430bc004128a672f36
https://doi.org/10.1021/acs.jpcb.2c06478
https://doi.org/10.1021/acs.jpcb.2c06478
Publikováno v:
ACS Omega. 7:43337-43345
The formation of amyloids due to the self-assembly of intrinsically disordered proteins or peptides is a hallmark for different neurodegenerative diseases. For example, amyloids formed by the amyloid beta (Aβ) peptides are responsible for the most d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dca237144e5aeafae414b977eab9d3f4
https://doi.org/10.1021/acsomega.2c06235
https://doi.org/10.1021/acsomega.2c06235
Publikováno v:
The Journal of Physical Chemistry B. 126:7271-7285
Room temperature molecular dynamics (MD) simulations of the globular protein α-lactalbumin in aqueous solutions containing BMIM (1-butyl-3-methylimidazolium) based ionic liquids (ILs) with a series of Hofmeister anions have been carried out. In part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb4037b3e79f6d8f5be1de18a80e27e
https://doi.org/10.1021/acs.jpcb.2c03940
https://doi.org/10.1021/acs.jpcb.2c03940
Publikováno v:
Journal of Chemical Information and Modeling. 62:3453-3462
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3d33ffa17fb2250a125b2c230c9e6b1
https://doi.org/10.1021/acs.jcim.2c00593
https://doi.org/10.1021/acs.jcim.2c00593
Molecular dynamics simulations have been carried out to explore the effect of complex formation between the N-terminal domain of the \la-repressor protein (in dimeric form) and the corresponding DNA operator on low-frequency intermolecular vibrationa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::510ec16eabd52e0ef8878942d6064408
https://doi.org/10.21203/rs.3.rs-2471243/v1
https://doi.org/10.21203/rs.3.rs-2471243/v1
Publikováno v:
Langmuir. 37:14429-14442
Aggregated form of α-synuclein in the brain has been found to be the major component of Lewy bodies that are hallmarks of Parkinson's disease (PD), the second most devastating neurodegenerative disorder. We have carried out room-temperature all-atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7647f76a6894ec8f14508ff4630633
https://doi.org/10.1021/acs.langmuir.1c02401
https://doi.org/10.1021/acs.langmuir.1c02401
Publikováno v:
Journal of chemical information and modeling. 62(8)
It is believed that water around an intrinsically disordered protein or peptide (IDP) in an aqueous environment plays an important role in guiding its conformational properties and aggregation behavior. However, despite its importance, only a handful
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75c0bc4b1dbe449e792c8b9b5889079a
https://pubmed.ncbi.nlm.nih.gov/35384652
https://pubmed.ncbi.nlm.nih.gov/35384652