Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Aswathy N. Muttathukattil"'
Publikováno v:
ACS Omega, Vol 3, Iss 10, Pp 14119-14126 (2018)
Externí odkaz:
https://doaj.org/article/781912ce567f493d87f2f166d8e23a6e
Publikováno v:
The journal of physical chemistry. B. 126(47)
Understanding the mechanism of ligands binding to their protein targets and the influence of various factors governing the binding thermodynamics is essential for rational drug design. The solution pH is one of the critical factors that can influence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e0d47f8f5dd9abbfaac0670717642f6
https://pubmed.ncbi.nlm.nih.gov/36383764
https://pubmed.ncbi.nlm.nih.gov/36383764
Understanding the mechanism of ligands binding to their protein targets and the influence of various factors governing the binding thermodynamics is essential for rational drug design. The solution pH is one of the critical factors that can influence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f226fc4f806695fcea48753a0301c3e
https://doi.org/10.1101/2022.07.01.498456
https://doi.org/10.1101/2022.07.01.498456
Publikováno v:
Current Opinion in Structural Biology. 60:101-109
Cells are equipped with cosolvents that modulate protein folding and aggregation to withstand water stress. The effect of cosolvents on the aggregation rates depends on whether the polypeptide sequence is an intrinsically disordered protein (IDP) or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4774e33891f157df7258f58cfa9026ed
https://doi.org/10.1016/j.sbi.2019.12.011
https://doi.org/10.1016/j.sbi.2019.12.011
Publikováno v:
The Journal of Physical Chemistry B. 123:9302-9311
Guanidinium cation (Gdm+) interacts strongly with amino acids of different polarities modulating protein structure and function. Using density functional theory calculations and molecular dynamics simulations, we studied the interaction of Gdm+ with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::984e151e35503719d3278c5984e51237
https://doi.org/10.1021/acs.jpcb.9b06130
https://doi.org/10.1021/acs.jpcb.9b06130
Publikováno v:
ACS Omega
ACS Omega, Vol 3, Iss 10, Pp 14119-14126 (2018)
ACS Omega, Vol 3, Iss 10, Pp 14119-14126 (2018)
Cosolvents play an important role in regulating the stability and function of proteins present in the cell. We studied the role of cosolvents, urea and guanidinium chloride (GdmCl), which act as protein denaturants, in the catalytic activity and stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9818c9710f6fd864f3bcc394046de33
http://europepmc.org/articles/PMC6644995
http://europepmc.org/articles/PMC6644995
Guanidinium cation (Gdm+) interacts strongly with amino acids of different polarities modulating protein structure and function. Using density functional theory calculations and molecular dynamics simulations we studied the interaction of Gdm+ with c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5940c64ed3822e52637889d7e0ee8606
https://doi.org/10.26434/chemrxiv.8425400
https://doi.org/10.26434/chemrxiv.8425400
Publikováno v:
The journal of physical chemistry. B. 123(15)
Disulfide bonds in proteins can strongly influence the folding pathways by constraining the conformational space. Hen egg white lysozyme has four disulfide bonds and is widely studied for its antibacterial properties. Experiments on lysozyme infer th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::947a060e741a1e5a16482a542073d5eb
https://pubmed.ncbi.nlm.nih.gov/30913878
https://pubmed.ncbi.nlm.nih.gov/30913878
Publikováno v:
The Journal of Physical Chemistry B. 120:10979-10989
Understanding the role of naturally occurring protective osmolytes, such as trimethylamine N-oxide (TMAO), in the growth of amyloid fibrils implicated in neurodegenerative diseases is important to prevent fibril growth. The effect of TMAO on the grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cb24feb7e2c2f91c65b83679590a400
https://doi.org/10.1021/acs.jpcb.6b09215
https://doi.org/10.1021/acs.jpcb.6b09215
Publikováno v:
The journal of physical chemistry letters. 9(17)
Salts differ in their ability to stabilize protein conformations, thereby affecting the thermodynamics and kinetics of protein folding. We developed a coarse-grained protein model that can predict salt-induced changes in protein properties by using t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85b1eea5b783b40effeb035a953a05f1
https://pubmed.ncbi.nlm.nih.gov/30130111
https://pubmed.ncbi.nlm.nih.gov/30130111