Results 111 to 120 of about 3,454,137 (301)

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad   +2 more
wiley   +1 more source

Dynamics of unfolded and [alpha]-helical polypeptide chains [PDF]

open access: yes, 2007
The aim of this thesis was the investigation of the dynamics of elementary steps in protein folding. During folding, the polypeptide chain explores the free energy surface and first interactions are established. These interactions lead to formation of
Fierz, Beat
core   +1 more source

Conformational dynamics between transmembrane domains and allosteric modulation of a metabotropic glutamate receptor

open access: yeseLife, 2019
Metabotropic glutamate receptors (mGluRs) are class C, synaptic G-protein-coupled receptors (GPCRs) that contain large extracellular ligand binding domains (LBDs) and form constitutive dimers.
Vanessa A Gutzeit   +6 more
doaj   +1 more source

Paclitaxel induces NM2‐dependent cellular contraction through GEF‐H1 dissociation from microtubules and RhoA/ROCK activation in cancer cells

open access: yesMolecular Oncology, EarlyView.
Taxanes are widely used chemotherapeutics whose effects on cellular mechanics remain poorly understood. We show that paclitaxel induces rapid cellular contraction by promoting GEF‐H1 dissociation from microtubules and non‐muscle myosin II activation through RhoA/ROCK.
Gloria Asensio‐Juárez   +5 more
wiley   +1 more source

Mapping Conformational Dynamics of Proteins Using Torsional Dynamics Simulations [PDF]

open access: yes, 2013
All-atom molecular dynamics simulations are widely used to study the flexibility of protein conformations. However, enhanced sampling techniques are required for simulating protein dynamics that occur on the millisecond timescale.
Vaidehi, Nagarajan   +4 more
core   +1 more source

Automated FRAP microscopy for high‐throughput analysis of protein dynamics in chromatin organization and transcription

open access: yesFEBS Open Bio, EarlyView.
RoboMic is an automated confocal microscopy pipeline for high‐throughput functional imaging in living cells. Demonstrated with fluorescence recovery after photobleaching (FRAP), it integrates AI‐driven nuclear segmentation, ROI selection, bleaching, and analysis.
Selçuk Yavuz   +6 more
wiley   +1 more source

Polarization‐resolved femtosecond Vis/IR spectroscopy tailored for resolving weak signals in biological samples using minimal sample volume

open access: yesFEBS Open Bio, EarlyView.
Unique biological samples, such as site‐specific mutant proteins, are available only in limited quantities. Here, we present a polarization‐resolved transient infrared spectroscopy setup with referencing to improve signal‐to‐noise tailored towards tracing small signals. We provide an overview of characterizing the excitation conditions for polarization‐
Clark Zahn, Karsten Heyne
wiley   +1 more source

A light‐triggered Time‐Resolved X‐ray Solution Scattering (TR‐XSS) workflow with application to protein conformational dynamics

open access: yesFEBS Open Bio, EarlyView.
Time‐resolved X‐ray solution scattering captures how proteins change shape in real time under near‐native conditions. This article presents a practical workflow for light‐triggered TR‐XSS experiments, from data collection to structural refinement. Using a calcium‐transporting membrane protein as an example, the approach can be broadly applied to study ...
Fatemeh Sabzian‐Molaei   +3 more
wiley   +1 more source

Conformational dynamics of tetraisopropylmethane and of tetracyclopropylmethane.

open access: yesJournal of the American Chemical Society, 2002
Tetraisopropylmethane (1) exists in solution as a mixture of two types of conformers (D2d and S4 time-averaged symmetry) in the ratio 93:7 at -110 degrees C, interconverting with a barrier of 9.7 kcal mol-1. Molecular mechanics calculations and the multiplicity of NMR signals at low temperature allow the assignment of these conformations.
Anderson, J. E.   +4 more
openaire   +2 more sources

Modeling conformational ensembles of slow functional motions in Pin1-WW.

open access: yesPLoS Computational Biology, 2010
Protein-protein interactions are often mediated by flexible loops that experience conformational dynamics on the microsecond to millisecond time scales. NMR relaxation studies can map these dynamics.
Faruck Morcos   +10 more
doaj   +1 more source

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