Experimental validation of theoretical models for protein electrostatics remains rare. Recently, we have developed a paramagnetic NMR-based method for de novo determination of effective near-surface electrostatic potentials, which allows for straightforward examination of electrostatic models for biomolecules. In the current work, we expand this method and demonstrate that effective near-surface electrostatic potentials can readily be determined from ¹H paramagnetic relaxation enhancement (PRE)...
NMR spectroscopy charges into protein surface electrostatics [Biophysics and Computational Biology]
NMR spectroscopy charges into protein surface electrostatics
Frans A. A. Mulder...
Date: 2021-07-22
Life needs interaction. The current pandemic has made visible how much interaction, or lack thereof, means for the life of each and every one of us. The validity of this statement also extends to the tiny and invisible: Over the years, scientists have taken key steps to understand the interactions... Read More
PNAS:
Number: 30
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[ASAP] Net Charge and Nonpolar Content Guide the Identification of Folded and Prion Proteins
Net Charge and Nonpolar Content Guide the Identification of Folded and Prion Proteins
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01114/20200511/images/medium/bi9b01114_0014.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01114
http://feeds.feedburner.com/~r/acs/bichaw/~4/_6_Oea9fEw0
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05-12-2020 05:10 AM
[NMR paper] Contemporary NMR Studies of Protein Electrostatics.
Contemporary NMR Studies of Protein Electrostatics.
Related Articles Contemporary NMR Studies of Protein Electrostatics.
Annu Rev Biophys. 2015 Feb 26;
Authors: Hass MA, Mulder FA
Abstract
Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing...
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03-10-2015 07:22 PM
[NMR paper] Selective (15)N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy.
Selective (15)N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy.
Related Articles Selective (15)N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy.
J Biomol NMR. 2014 Jul 8;
Authors: Cao C, Chen JL, Yang Y, Huang F, Otting G, Su XC
Abstract
The side-chain amide groups of asparagine and glutamine play important roles in stabilizing the structural fold of proteins, participating in...
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Selective 15N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy
Selective 15N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy
Abstract
The side-chain amide groups of asparagine and glutamine play important roles in stabilizing the structural fold of proteins, participating in hydrogen-bonding networks and protein interactions. Selective 15N-labeling of side-chain amides, however, can be a challenge due to enzyme-catalyzed exchange of amide groups during protein synthesis. In the present study, we developed an efficient way of selectively...
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[NMR paper] Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and T
Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Related Articles Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Biochemistry. 1998 Dec 8;37(49):17318-30
Authors: Padmanabhan S, Jiménez MA, Laurents DV, Rico M
Interactions between side chains spaced (i,i + 3) and (i,i + 4) may explain the context dependence of helix propensities observed...
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11-17-2010 11:15 PM
[NMR paper] Measuring enzyme hydration in nonpolar organic solvents using NMR.
Measuring enzyme hydration in nonpolar organic solvents using NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Measuring enzyme hydration in nonpolar organic solvents using NMR.
Biotechnol Bioeng. 1995 Jun 5;46(5):452-8
Authors: Parker MC, Moore BD, Blacker AJ
A very sensitive NMR method has been developed for measuring deuterated water bound to proteins suspended in nonpolar solvents. This has been used to determine the amount of...
Protein Electrostatics Investigated through Paramagnetic NMR for Nonpolar Groups
Linear Mode
