Flavodoxin (Fld) is a small FMN containing protein that is involved in single electron transfer. The long-chain flavodoxin in Rhodopseudomonas palustris bacteria replaces ferredoxin as a low-potential electron carrier when iron is scarce. Thus it is proposed to interact with the bifurcating electron transfer flavoprotein (ETF) that yields low-potential electrons. A surface loop on Fld interacts with another of Fld's partner proteins, so we hypothesize that it also mediates Fld's interaction with...
[NMR paper] Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy
Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy
The folding of many proteins can begin during biosynthesis on the ribosome and can be modulated by the ribosome itself. Such perturbations are generally believed to be mediated through interactions between the nascent chain and the ribosome surface, but despite recent progress in characterising interactions of unfolded states with the ribosome, and their impact on the initiation of co-translational folding, a complete quantitative analysis of interactions across both...
nmrlearner
Journal club
0
11-09-2021 10:05 AM
[NMR paper] Assignments of (19)F NMR resonances and exploration of dynamics in a long-chain flavodoxin
Assignments of (19)F NMR resonances and exploration of dynamics in a long-chain flavodoxin
Flavodoxin is a small protein that employs a non-covalently bound flavin to mediate single-electron transfer at low potentials. The long-chain flavodoxins possess a long surface loop that is proposed to interact with partner proteins. We have incorporated ^(19)F-labeled tyrosine in long-chain flavodoxin from Rhodopseudomonas palustris to gain a probe of possible loop dynamics, exploiting the presence of a Tyr in the long loop in addition to Tyr residues near the flavin. We report ^(19)F...
More...
nmrlearner
Journal club
0
03-18-2021 05:17 PM
[NMR paper] Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Related Articles Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Chem Phys Lipids. 2021 Feb 15;:105062
Authors: Chang Z, Deng J, Zhao W, Yang J
Abstract
A hallmark of Alzheimer's, Parkinson's, and other amyloid diseases is the assembly of amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and cytotoxicity...
nmrlearner
Journal club
0
02-20-2021 07:45 PM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/QJjXPpa0z9I
More...
nmrlearner
Journal club
0
07-06-2018 09:40 AM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/QJjXPpa0z9I
More...
nmrlearner
Journal club
0
07-06-2018 09:40 AM
[NMR paper] Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.
Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.
J Phys Chem B. 2016 07 21;120(28):6951-60
Authors: Paz Ramos A, Lagüe P, Lamoureux G, Lafleur M
...
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 25 October 2011</br>
Woo Sung*Son, Sang Ho*Park, Henry J.*Nothnagel, George J.*Lu, Yan*Wang, ...</br>
‘q-titration’ refers to the systematic comparison of signal intensities in solution NMR spectra of uniformlyN labeled membrane proteins solubilized in micelles and isotropic bicelles as a function of the molar ratios (q) of the...
Applying Crystallography and 19 F NMR to investigate dynamics and partner protein interactions in a long chain Flavodoxin
Linear Mode
