Pressure Dependence of Side Chain H and N-chemical Shifts in the Model Peptides Ac-Gly-Gly-Xxx-Ala-NH

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2020 Jun 24

PMID 32572797

Citations 2

Authors

Markus Beck Erlach

Joerg Koehler

Claudia E Munte

Werner Kremer

Edson Crusca Jr

Masatsune Kainosho

Hans Robert Kalbitzer

Affiliations

Soon will be listed here.

Abstract

For interpreting the pressure induced shifts of resonance lines of folded as well as unfolded proteins the availability of data from well-defined model systems is indispensable. Here, we report the pressure dependence of H and N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH (Xxx is one of the 20 canonical amino acids) measured at 800 MHz proton frequency. As observed earlier for other nuclei the chemical shifts of the side chain nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200 MPa. The pressure response is described by a second degree polynomial with the pressure coefficients B and B that are dependent on the atom type and type of amino acid studied. A number of resonances could be assigned stereospecifically including the H and N resonances of the guanidine group of arginine. In addition, stereoselectively isotope labeled SAIL amino acids were used to support the stereochemical assignments. The random-coil pressure coefficients are also dependent on the neighbor in the sequence as an analysis of the data shows. For H and H correction factors for different amino acids were derived. In addition, a simple correction of compression effects in thermodynamic analysis of structural transitions in proteins was derived on the basis of random-coil pressure coefficients.

Citing Articles

Solution structure and pressure response of thioredoxin-1 of Plasmodium falciparum.

Munte C, Kalbitzer H PLoS One. 2024; 19(4):e0301579.

PMID: 38635664 PMC: 11025842. DOI: 10.1371/journal.pone.0301579.

The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.

Kovacs D, Bodor A RSC Adv. 2023; 13(15):10182-10203.

PMID: 37006359 PMC: 10065145. DOI: 10.1039/d3ra00977g.

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