Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Barbara Hribar-Lee"'
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
Publikováno v:
Biomolecules, Vol 13, Iss 12, p 1703 (2023)
Protein molecules associate in solution, often in clusters beyond pairwise, leading to liquid phase separations and high viscosities. It is often impractical to study these multi-protein systems by atomistic computer simulations, particularly in mult
Externí odkaz:
https://doaj.org/article/075cf08056564076b685aaf44a321a62
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
Publikováno v:
Pharmaceutics, Vol 15, Iss 1, p 119 (2022)
Identifying binding sites on the protein surface is an important part of computer-assisted drug design processes. Reliable prediction of binding sites not only assists with docking algorithms, but it can also explain the possible side-effects of a po
Externí odkaz:
https://doaj.org/article/91bbe74173c346f8a6b95e9cc9b2218d
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:
Molecules, Vol 27, Iss 3, p 999 (2022)
Pharmaceutical design of protein formulations aims at maximum efficiency (protein concentration) and minimum viscosity. Therefore, it is important to know the nature of protein-protein interactions and their influence on viscosity. In this work, we i
Externí odkaz:
https://doaj.org/article/3aa4aa23863241e28e37ab07b86a6d38
Publikováno v:
Acta Chimica Slovenica, Vol 64, Iss 3, Pp 560-563 (2017)
Calculations of molecular electrostatic potential were correlated with experimental pKa values for different sets of acidic molecules (carboxylic acids, phenols, and anilines) to obtain linear relationships of variable quality. A single tri-parameter
Externí odkaz:
https://doaj.org/article/1eda5d8ea0d8468dac4e09b1c9fec79a
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
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