Cyclization can stabilize the structure of proteins, as previously demonstrated in single-domain proteins. Although Lys48-linked polyubiquitin, a multi-domain protein, is also known to be cyclized in human cells, the structural effects of cyclization remain unclear. Here, we examined the impact of cyclization on the structural stability and dynamics of cyclic Lys48-linked diubiquitin (Ub(2) ). As expected, cyclization increased the thermal stability of Ub(2) and its resistance to proteolytic...
An integrated approach of NMR experiments and MD simulations visualizes structural dynamics of a cyclic multi-domain protein
An integrated approach of NMR experiments and MD simulations visualizes structural dynamics of a cyclic multi-domain protein
Abstract
Cyclization can stabilize the structure of proteins, as previously demonstrated in single-domain proteins. Although Lys48-linked polyubiquitin, a multi-domain protein, is also known to be cyclized in human cells, the structural effects of cyclization remain unclear. Here, we examined the impact of cyclization on the structural stability and dynamics of cyclic Lys48-linked diubiquitin (Ub2). As expected, cyclization increased the thermal stability of Ub2...
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08-26-2023 09:35 PM
[NMR paper] Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach
Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach
The bacterial pathogen Vibrio cholerae use a type III secretion system to inject effector proteins into a host cell. Recently, a putative Toxic GTPase Activating Protein (ToxGAP) called VopE was identified as a T3SS substrate and virulence factor that affected host mitochondrial dynamics and immune response. However, biophysical and structural characterization has been absent. Here, we describe solution NMR structure of the putative GAP domain (73-204) of...
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02-10-2022 09:59 AM
Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach
Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach
Abstract
The bacterial pathogen Vibrio cholerae use a type III secretion system to inject effector proteins into a host cell. Recently, a putative Toxic GTPase Activating Protein (ToxGAP) called VopE was identified as a T3SS substrate and virulence factor that affected host mitochondrial dynamics and immune response. However, biophysical and structural characterization has been absent. Here, we describe solution NMR structure of the putative GAP domain...
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02-09-2022 05:00 PM
[NMR paper] Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.
Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--cdn.elifesciences.org-images-elife_oa@1x.png Related Articles Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.
Elife. 2020 Jul 30;9:
Authors: Bengtsen T, Holm VL, Kjølbye LR, Midtgaard SR, Johansen NT, Tesei G, Bottaro S, Schiøtt B, Arleth L, Lindorff-Larsen K
Abstract
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08-01-2020 02:01 PM
Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach
Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach
Abstract
The insertase BamA is an essential protein of the bacterial outer membrane. Its 16-stranded transmembrane β-barrel contains a lateral gate as a key functional element. This gate is formed by the C-terminal half of the last β-strand. The BamA barrel was previously found to sample different conformations in aqueous solution, as well as different gate-open, gate-closed, and collapsed conformations in...
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05-09-2019 05:55 AM
How to tackle protein structural data from solution and solid state: An integrated approach
How to tackle protein structural data from solution and solid state: An integrated approach
Publication date: February 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 92–93</br>
Author(s): Azzurra Carlon, Enrico Ravera, Witold Andra?oj?, Giacomo Parigi, Garib N. Murshudov, Claudio Luchinat</br>
Long-range NMR restraints, such as diamagnetic residual dipolar couplings and paramagnetic data, can be used to determine 3D structures of macromolecules. They are also used to monitor, and potentially to improve, the accuracy of a...
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04-09-2016 03:54 AM
Rice University Researchers' New Integrated Approach Predicts Structural ... - BioNews Texas
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Rice University Researchers' New Integrated Approach Predicts Structural ...
BioNews Texas
The most common methods for protein structural analysis currently are X-ray crystallography and nuclear magnetic resonance spectroscopy (NMR), however, these do not provide information about how proteins change their forms from native to functional ...
Rice University Researchers' New Integrated Approach Predicts Structural ... - BioNews Texas
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An integrated approach of NMR experiments and MD simulations visualizes structural dynamics of a cyclic multi-domain protein
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