Inherent dynamics of maltose binding protein (MBP) are immune to the native environment.
Thoma, J.; Burmann, B. M.
Show abstract
Biophysical characterizations of proteins typically rely on a reductionistic approach, studying proteins in a highly purified from and in absence of their natural cellular environment. Little is known about how the highly crowded conditions prevalent within living cells influence the dynamic structures proteins on the molecular level. To address this outstanding question, we characterize here the dynamic behavior of the periplasmic model protein MBP from Escherichia coli in situ, confined in the native lumen of bacterial outer membrane vesicles. To this end we determine the dynamics of side-chain methyl groups of MBP across several timescales and compare them to purified in vitro MBP. We find that the inherent dynamics of MBP are surprisingly insensitive to the native cellular environment and that the molecular motion of the protein is mainly impacted on a global level.
Matching journals
The top 1 journal accounts for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Dynamic structural order of a low complexity domain facilitates assembly of intermediate filaments 95%
- In-cell destabilization of a homo-dimeric protein complex detected by DEER spectroscopy 94%
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA 93%
Similar papers in this journal
- Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone and side-chains in EL222 92%
- A High-Sensitivity Stopped-Flow EPR System to Monitor Millisecond Conformational Kinetics in Spin-Labeled Proteins 92%
- Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions 92%
Similar papers in this journal
- Preferential interactions of a crowder protein with the specific binding site of a native protein complex 95%
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: a Single-Molecule FRET Study 92%
- Integrated assessment of structure and dynamics of solid proteins via accurate solid-state NMR distance information 90%
Similar papers in this journal
- Genetically encoded phase contrast agents for digital holographic microscopy 90%
- Imaging transmembrane dynamics of biomolecules at live cell plasma membranes using quenchers in extracellular environment 89%
- Single-molecule displacement mapping unveils sign-asymmetric protein charge effects on intraorganellar diffusion 89%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.