Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Sandi, Brudar"'
Autor:
Sandi Brudar, Leonid Breydo, Elisha Chung, Ken A. Dill, Nasim Ehterami, Ketan Phadnis, Samir Senapati, Mohammed Shameem, Xiaolin Tang, Muhammmad Tayyab, Barbara Hribar-Lee
Publikováno v:
mAbs, Vol 16, Iss 1 (2024)
ABSTRACTUnderstanding factors that affect the clustering and association of antibodies molecules in solution is critical to their development as therapeutics. For 19 different monoclonal antibody (mAb) solutions, we measured the viscosities, the seco
Externí odkaz:
https://doaj.org/article/8d762b7c24c345f59e346532165988ed
Autor:
Sandi Brudar, Barbara Hribar-Lee
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 2, p 1197 (2023)
The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the additi
Externí odkaz:
https://doaj.org/article/a713f72e2cf34c86a26f96f227b339b9
Autor:
Mina Nikolić, Sandi Brudar, Evangelos Coutsias, Ken A. Dill, Miha Lukšič, Carlos Simmerling, Barbara Hribar-Lee
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 23, p 15371 (2022)
We present here a freely available web-based database, called BioMThermDB 1.0, of thermophysical and dynamic properties of various proteins and their aqueous solutions. It contains the hydrodynamic radius, electrophoretic mobility, zeta potential, se
Externí odkaz:
https://doaj.org/article/6ac29dff5baa4be6a75cf7604dbd6fd1
Publikováno v:
Acta Chimica Slovenica, Vol 64, Iss 3, Pp 564-570 (2017)
Differential scanning calorimetry provides unique signatures of blood plasma samples. Plasma samples from diseased individuals yield specific thermograms, which differ from each other and from plasma samples of healthy individuals. Thermograms from i
Externí odkaz:
https://doaj.org/article/f667bcea673c446facc758b025386b14
Autor:
Sandi, Brudar, Barbara, Hribar-Lee
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2551
The amyloidophilic dyes thioflavin T and Congo red are small, yet powerful, molecules that allow the in vitro and in vivo detection of amyloid fibrils in protein solutions. Even though Congo red and thioflavin T binding assays are widespread techniqu
Autor:
Sandi Brudar, Barbara Hribar-Lee
Publikováno v:
Methods in Molecular Biology ISBN: 9781071625965
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7ca908e88db3f0ac7621c37b34fbf36
https://doi.org/10.1007/978-1-0716-2597-2_19
https://doi.org/10.1007/978-1-0716-2597-2_19
Autor:
Barbara Hribar-Lee, Sandi Brudar
Publikováno v:
The Journal of Physical Chemistry. B
Liquid-liquid phase separation (LLPS) of proteins has recently been associated with the onset of numerous diseases. Despite several studies in this area of protein aggregation, buffer-specific effects always seem to be overlooked. In this study we in
Autor:
Sandi Brudar, Barbara Hribar-Lee
Publikováno v:
Biomolecules, Vol 9, Iss 2, p 65 (2019)
Amyloid fibrils, highly ordered protein aggregates, play an important role in the onset of several neurological disorders. Many studies have assessed amyloid fibril formation under specific solution conditions, but they all lack an important phenomen
Externí odkaz:
https://doaj.org/article/dad29a18d17544a1b890b87d192350dc
Proteins are the most abundant biomacromolecules in living cells, where they perform vital roles in virtually every biological process. To maintain their function, proteins need to remain in a stable (native) state. Inter- and intramolecular interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a660f828e25eee79559ce3f1842301de
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85099237836
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85099237836
Publikováno v:
Phys Chem Chem Phys
Proteins are the most abundant biomacromolecules in living cells, where they perform vital roles in virtually every biological process. To maintain their function, proteins need to remain in a stable (native) state. Inter- and intramolecular interact