activity
20172026
most citedCrowding-induced Elongated Conformation of Urea-unfolded Apoazurin: Investigating the Role of Crowder Shape In Silico

30 citations · 71 across the 6 of their papers we have counts for

collaborators

6 papers

q-bio.BM2026

Physical principles of building protein megacomplexes in a crowded milieu

Jiayi Wang, Jules Nde, Andrei G. Gasic +2

Multiple phenotypic protein expressions arising from one genome represent variations in the protein relative abundance and their stoichiometry. A lack of definite compositional par…

q-bio.BM2021★ 4 cited

Understanding Protein-Complex Assembly through Grand Canonical Maximum Entropy Modeling

Andrei G. Gasic, Atrayee Sarkar, Margaret S. Cheung

Inside a cell, heterotypic proteins assemble in inhomogeneous, crowded systems where the abundance of these proteins vary with cell types. While some protein complexes form putativ…

q-bio.BM2019★ 9 cited

A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior Under High Hydrostatic Pressure

Andrei G. Gasic, Margaret S. Cheung

Hydrostatic pressure is a common perturbation to probe the conformations of proteins. There are two common forms of pressure dependent potentials of mean force (PMFs) derived from…

q-bio.BM2019★ 17 cited

Critical phenomena in the temperature-pressure-crowding phase diagram of a protein

Andrei G. Gasic, Mayank M. Boob, Maxim B. Prigozhin +4

In the cell, proteins fold and perform complex functions through global structural rearrangements. Function requires a protein to be at the brink of stability to be susceptible to…

q-bio.BM2019★ 30 cited

Crowding-induced Elongated Conformation of Urea-unfolded Apoazurin: Investigating the Role of Crowder Shape In Silico

Fabio C. Zegarra, Dirar Homouz, Andrei G. Gasic +4

Here, we show by solution nuclear magnetic resonance measurements that the urea-unfolded protein apoazurin becomes elongated when the synthetic crowding agent dextran 20 is present…

q-bio.BM2017★ 11 cited

The impact of hydrodynamic interactions on protein folding rates depends on temperature

Fabio C. Zegarra, Dirar Homouz, Yossi Eliaz +2

We investigated the impact of hydrodynamic interactions (HI) on protein folding using a coarse-grained model. The extent of the impact of hydrodynamic interactions, whether it acce…