Impact of cellular crowding on protein structural dynamics investigated by EPR spectroscopy
The study of how the intracellular medium influences protein structural dynamics and protein–
protein interactions is a captivating area of research for scientists aiming to comprehend …
protein interactions is a captivating area of research for scientists aiming to comprehend …
Integrating Electron Paramagnetic Resonance Spectroscopy and Computational Modeling to Measure Protein Structure and Dynamics
Electron paramagnetic resonance (EPR) has become a powerful probe of conformational
heterogeneity and dynamics of biomolecules. In this Review, we discuss different …
heterogeneity and dynamics of biomolecules. In this Review, we discuss different …
Differentiating between Label and Protein Conformers in Pulsed Dipolar EPR Spectroscopy with the dHis‐Cu2+(NTA) Motif
CA Heubach, Z Hasanbasri, D Abdullin… - … A European Journal, 2023 - Wiley Online Library
Pulsed dipolar EPR spectroscopy (PDS) in combination with site‐directed spin labeling is a
powerful tool in structural biology. However, the commonly used spin labels are conjugated …
powerful tool in structural biology. However, the commonly used spin labels are conjugated …
Endogenous Cu (II) labeling for distance measurements on proteins by EPR
HR Hunter, S Kankati, Z Hasanbasri… - … –A European Journal, 2024 - Wiley Online Library
In‐cell measurements of the relationship between structure and dynamics to protein function
is at the forefront of biophysics. Recently, developments in EPR methodology have …
is at the forefront of biophysics. Recently, developments in EPR methodology have …
Modeling of Cu (ii)-based protein spin labels using rotamer libraries
Z Hasanbasri, MH Tessmer, S Stoll… - Physical Chemistry …, 2024 - pubs.rsc.org
The bifunctional spin label double-histidine copper-(II) capped with nitrilotriacetate [dHis-Cu
(II)-NTA], used in conjunction with electron paramagnetic resonance (EPR) methods can …
(II)-NTA], used in conjunction with electron paramagnetic resonance (EPR) methods can …
Measurement of protein dynamics from site directed Cu (II) labeling
K Singewald, H Hunter, TF Cunningham… - Analysis & …, 2023 - Wiley Online Library
This review describes the use of Electron Paramagnetic Resonance (EPR) to measure
residue specific dynamics in proteins with a specific focus on Cu (II)‐based spin labels. First …
residue specific dynamics in proteins with a specific focus on Cu (II)‐based spin labels. First …
The use of EPR spectroscopy to study transcription mechanisms
Electron paramagnetic resonance (EPR) spectroscopy has become a promising structural
biology tool to resolve complex and dynamic biological mechanisms in-vitro and in-cell …
biology tool to resolve complex and dynamic biological mechanisms in-vitro and in-cell …
The chromatin remodeler SMARCA5 binds to d-block metal supports: Characterization of affinities by IMAC chromatography and QM analysis
PC Andrikopoulos, P Čabart - Plos one, 2024 - journals.plos.org
The ISWI family protein SMARCA5 contains the ATP-binding pocket that coordinates the
catalytic Mg2+ ion and water molecules for ATP hydrolysis. In this study, we demonstrate …
catalytic Mg2+ ion and water molecules for ATP hydrolysis. In this study, we demonstrate …
PELDOR to the Metal: Cu (II)-Based Labels Put a New Spin on Distance Measurements
J Casto, S Palit, S Saxena - Applied Magnetic Resonance, 2024 - Springer
Eighty years ago, the advent of electron paramagnetic resonance (EPR) revolutionized our
ability to observe the physical world of unpaired electron spins. The inception of EPR …
ability to observe the physical world of unpaired electron spins. The inception of EPR …
SITE DIRECTED LABELING STRATEGIES TO PROBE PROTEIN DYNAMICS AND IN VIVO DISTANCE CONSTRAINTS
K Singewald - 2024 - d-scholarship.pitt.edu
This thesis describes the use of Electron Paramagnetic Resonance (EPR) to measure
residue specific dynamics in proteins with a specific focus on Cu (II)-based spin labels …
residue specific dynamics in proteins with a specific focus on Cu (II)-based spin labels …