Understanding the structure and dynamics of biological macromolecules is essential to decipher the molecular mechanisms that underlie cellular functions. The description of structure and conformational dynamics often requires the integration of complementary techniques. In this review, we highlight the utility of combining nuclear magnetic resonance (NMR) spectroscopy with small angle scattering (SAS) to characterize these challenging biomolecular systems. NMR can assess the structure and...
[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] A hybrid strategy combining solution NMR spectroscopy and isothermal titration calorimetry to characterize protein-nanodisc interaction
A hybrid strategy combining solution NMR spectroscopy and isothermal titration calorimetry to characterize protein-nanodisc interaction
NMR is a powerful tool for characterizing intermolecular interactions at atomic resolution. However, the nature of the complex interactions of membrane-binding proteins makes it difficult to elucidate the interaction mechanisms. Here, we demonstrated that structural and thermodynamic analyses using solution NMR spectroscopy and isothermal titration calorimetry (ITC) can clearly detect a specific interaction between the pleckstrin homology (PH) domain of...
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12-15-2021 08:31 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
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein
Publication date: 27 February 2018
Source:Biophysical Journal, Volume 114, Issue 4</br>
Author(s): Karl T. Debiec, Matthew J. Whitley, Leonardus M.I. Koharudin, Lillian T. Chong, Angela M. Gronenborn</br>
Multidomain proteins with two or more independently folded functional domains are prevalent in nature. Whereas most multidomain proteins are linked linearly in sequence, roughly one-tenth possess domain insertions where a guest domain is implanted into a loop...
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03-03-2018 12:01 PM
[NMR paper] Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.
Biophys J. 2018 Feb 27;114(4):839-855
Authors: Debiec KT, Whitley MJ, Koharudin LMI, Chong LT, Gronenborn AM
Abstract
Multidomain proteins with two or more independently folded functional domains are prevalent in nature. Whereas most multidomain proteins are linked linearly in sequence, roughly one-tenth possess domain insertions where...
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03-01-2018 09:20 PM
Combining H/D Exchange Mass Spectrometry and ComputationalDocking To Derive the Structure of Protein–Protein Complexes
Combining H/D Exchange Mass Spectrometry and ComputationalDocking To Derive the Structure of Protein–Protein Complexes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00643/20171116/images/medium/bi-2017-00643w_0002.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00643
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/RQv07eLEF3A
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11-20-2017 02:16 PM
[NMR paper] Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Related Articles Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Methods Enzymol. 2015;558:279-331
Authors: Duss O, Yulikov M, Allain FH, Jeschke G
Abstract
Although functional significance of large noncoding RNAs and their complexes with proteins is well recognized, structural information for this class of systems is very scarce. Their inherent flexibility causes problems in...
Combining NMR, SAXS and SANS to characterize the structure and dynamics of protein complexes
Linear Mode
