Results 51 to 60 of about 3,454,137 (301)
Summary: The AAA+ ATPase complex on proteasome powers its functions through a series of intricate conformational transitions. Here, we describe a procedure to simulate the conformational dynamics of the proteasomal ATPase complex.
Rui Fang, Ying Lu
doaj +1 more source
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source
Conformational Dynamics Simulations of Proteins [PDF]
Molecular dynamics (MD) simulations of proteins provide descriptions of atomic motions, which allow to relate observable properties of proteins to microscopic processes. Unfortunately, such MD simulations require an enormous amount of computer time and, therefore, are limited to time scales of nanoseconds.
Eichinger, Markus +10 more
openaire +2 more sources
Dynamozones are the most obvious sign of the evolution of conformational dynamics in HIV-1 protease
Proteins are not static but are flexible molecules that can adopt many different conformations. The HIV-1 protease is an important target for the development of therapies to treat AIDS, due to its critical role in the viral life cycle.
Mohammad Rahimi +2 more
doaj +1 more source
Biophysical approaches for studying viral entry
Viruses infect all living organisms and have been responsible for major epidemics and pandemics. Their ongoing evolutionary battle with host defenses creates a constant need for improved tools to study viral behavior. Advancing methods to probe viral attachment, fusion, and genome release deepen our understanding of how infections begin and support the
Inbar Yosibash, Raya Sorkin
wiley +1 more source
The dynamics of excited‐state charge transfer (CT) in second near‐infrared (NIR‐II) fluorophore proceeds with conformational change that govern fluorescence.
Minghui Li +11 more
doaj +1 more source
Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto +3 more
wiley +1 more source
Conformational dynamics of the pyrene excimer
We characterized the S 1 state PES of the pyrene dimer, revealing key excimer conformations. A rapid shift to a stacked-twisted form dominates the excimer's structure and fluorescence.
Giovanni Parolin +5 more
openaire +4 more sources
Origin of conformational dynamics in a globular protein [PDF]
Abstract Protein structures are dynamic, undergoing motions that can play a vital role in function. However, the link between primary sequence and conformational dynamics remains poorly understood. Here, we studied how conformational dynamics can arise in a globular protein by evaluating the impact of individual core-residue ...
Damry, Adam M. +4 more
openaire +2 more sources
Molecular dynamics simulation of the follicle-stimulating hormone receptor. Understanding the conformational dynamics of receptor variants at positions N680 and D408 from in silico analysis. [PDF]
Follicle-stimulating hormone receptor (FSHR) is a G-protein coupled receptor (GPCR) and a prototype of the glycoprotein hormone receptors subfamily of GPCRs.
Eduardo Jardón-Valadez +5 more
doaj +1 more source

