Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Upayan Baul"'
Autor:
Wade F. Zeno, Upayan Baul, Wilton T. Snead, Andre C. M. DeGroot, Liping Wang, Eileen M. Lafer, D. Thirumalai, Jeanne C. Stachowiak
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Many proteins which sense membrane curvature contain intrinsically disordered domains. Here the authors use Monte Carlo simulations combined with experimental approaches and report that disordered domains are potent sensors of membrane curvature.
Externí odkaz:
https://doaj.org/article/5f61987e274540b184a22aa18a68b20c
We study the influence of intrinsic noise on the structure and dynamics of responsive colloids (RCs) which actively change their size and mutual interactions. The colloidal size is explicitly resolved in our RC model as an internal degree of freedom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51b370118519802a197298698b9d1b41
http://arxiv.org/abs/2211.14164
http://arxiv.org/abs/2211.14164
Publikováno v:
Physical review. E. 106(1-1)
We introduce a model of active responsive colloids (ARCs) in which an internal degree of freedom (DoF) of a single colloidal particle is "activated" by coupling it to a different thermostat than for the translational DoFs. As for the responsive inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afdbf4a65fba291daacafbd75660d000
https://pubmed.ncbi.nlm.nih.gov/35974513
https://pubmed.ncbi.nlm.nih.gov/35974513
Publikováno v:
Physical review. E. 104(3-1)
A fundamental paradigm in polymer physics is that macromolecular conformations in equilibrium can be described by universal scaling laws, being key for structure, dynamics, and function of soft (biological) matter and in the materials sciences. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b33dfeb2566f8baf1bdddc1101cfac4e
https://pubmed.ncbi.nlm.nih.gov/34654077
https://pubmed.ncbi.nlm.nih.gov/34654077
Publikováno v:
Biomacromolecules
Elastin-like polypeptides (ELPs) undergo a sharp solubility transition from low temperature solvated phases to coacervates at elevated temperatures, driven by the increased strength of hydrophobic interactions at higher temperatures. The transition t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acc64f7d5f721fe312a0e8f4d640c006
Autor:
Satyavani Vemparala, Upayan Baul
Publikováno v:
Antimicrobial Materials for Biomedical Applications ISBN: 9781788011884
Increased levels of antibiotic drug resistance of virulent bacteria is an urgent healthcare issue that needs to be rethought, not in terms of producing more potent antibiotics, but requiring a paradigm shift. A class of small proteins called host def
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2d28c2051370592ecfacec6facb9f02
https://doi.org/10.1039/9781788012638-00113
https://doi.org/10.1039/9781788012638-00113
Extensive molecular dynamics simulations have been employed to probe the effects of salts on the kinetics and dynamics of early-stage aggregated structures of steric zipper peptides in water. The simulations reveal that the chemical identity and vale
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e9d05e9288ce2684c871adc8d036866
https://doi.org/10.1101/649004
https://doi.org/10.1101/649004
Autor:
Wilton T. Snead, Andre C.M. DeGroot, D. Thirumalai, Wade F. Zeno, Eileen M. Lafer, Jeanne C. Stachowiak, Liping Wang, Upayan Baul
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
The ability of proteins to sense membrane curvature is essential to cellular function. All known sensing mechanisms rely on protein domains with specific structural features such as wedge-like amphipathic helices and crescent-shaped BAR domains. Yet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70cca5c7e69d2f3ea754fa053bca0256
https://doi.org/10.1038/s41467-018-06532-3
https://doi.org/10.1038/s41467-018-06532-3
Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structures, thus challenging the archetypal notion of structure-function relationships. Determining the ensemble of conformations that IDPs explore under physiological condi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a94eb43c956f88b8098a7a0f28e3056f
Autor:
Mohini M. Konai, L. W. Hamoen, Jayanta Haldar, Priyank Singh, Sandip Samaddar, Upayan Baul, Divakara S. S. M. Uppu, T. K. Siersma, Chandrabhas Narayana, Satyavani Vemparala
Publikováno v:
Chemical Science. 7:4613-4623
Biomimetic antibacterial polymers, the functional mimics of antimicrobial peptides (AMPs), targeting the bacterial cell membrane have been developed to combat the problem of antibiotic resistance. Amphiphilicity, a balance of cationic charge and hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63d7dfecdfc3f4d068874691bd93d0cd
https://doi.org/10.1039/c6sc00615a
https://doi.org/10.1039/c6sc00615a