Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Blake B. Langdon"'
Autor:
Indira Sriram, Yanxia Zhang, Ajay R. Lajmi, Blake B. Langdon, Daniel K. Schwartz, Roya B. Mirhossaini, Orlando J. Rojas, Joshua N. Mabry
Publikováno v:
ACS APPLIED MATERIALS AND INTERFACES. 7(6):3607-3617
Although polymeric membranes are widely used in the purification of protein pharmaceuticals, interactions between biomolecules and membrane surfaces can lead to reduced membrane performance and damage to the product. In this study, single-molecule fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff53ace6bf2a5b51e94b66ac07adf41d
https://doi.org/10.1021/am507730k
https://doi.org/10.1021/am507730k
Publikováno v:
Advances in Colloid and Interface Science. 207:240-252
A common goal across different fields (e.g. separations, biosensors, biomaterials, pharmaceuticals) is to understand how protein behavior at solid-liquid interfaces is affected by environmental conditions. Temperature, pH, ionic strength, and the che
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e9e755aae4a837d8334c010eed8d8d9
https://doi.org/10.1016/j.cis.2013.12.006
https://doi.org/10.1016/j.cis.2013.12.006
Publikováno v:
The Electricity Journal. 24:63-71
Electricity storage technologies are stymied by regulatory markets that are unable to fully monetize their benefits. Regulatory changes are needed. These changes include breaking out ancillary services from generation for purposes of planning and bid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a85f397233708393cec2a027cbf3a67e
https://doi.org/10.1016/j.tej.2011.06.006
https://doi.org/10.1016/j.tej.2011.06.006
Publikováno v:
Biomacromolecules. 16(10)
Surface chemistry modifications have been exploited in many applications in order to tune protein adsorption, layer formation, and aggregation. However, the kinetic processes by which surface chemistry influences protein adsorption and aggregation re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e6079989e0b17a46cffedbb0d410413
https://pubmed.ncbi.nlm.nih.gov/26327275
https://pubmed.ncbi.nlm.nih.gov/26327275
While traditional models of protein adsorption focus primarily on direct protein-surface interactions, recent findings suggest that protein-protein interactions may play a central role. Using high-throughput intermolecular resonance energy transfer (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d079c0a332259ed691995c484ee57a0d
https://europepmc.org/articles/PMC3895929/
https://europepmc.org/articles/PMC3895929/
Publikováno v:
Journal of the American Chemical Society. 133(13)
Through the use of single-molecule total internal reflection fluorescence microscopy, the dynamic behavior of fibrinogen was observed at the interface between aqueous solution and various solid surfaces. Multiple populations of objects were observed,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1913e95c354842200f2e687cf7b55314
https://pubmed.ncbi.nlm.nih.gov/21391676
https://pubmed.ncbi.nlm.nih.gov/21391676
Publikováno v:
Biophysical Journal. (11):2625-2633
With the use of single-molecule total internal reflection fluorescence microscopy (TIRFM), the dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observed at the solid-aqueous interface as a function of temper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed5ae2712484bad91e0208865ecb58db