Pressure dependence of side chain H-1 and N-15-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2

Author(s)

Erlach, Markus Beck ; Koehler, Joerg ; Munte, Claudia E. ; Kremer, Werner ; Crusca, Edson, Jr. ; Kainosho, Masatsune ; Kalbitzer, Hans Robert

• Document type: Journal article
• Source: Journal of Biomolecular NMR; v. 74, n. 8-9, p. 19-pg., 2020-06-22.

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(1)H and(15)N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2(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 coefficientsB(1)andB(2)that are dependent on the atom type and type of amino acid studied. A number of resonances could be assigned stereospecifically including the(1)H and(15)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(alpha)and H(N)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. (AU)

• FAPESP's process: 10/12953-4 - Structural determination of the C-terminal domains of septins SEPT2 and SEPT4 and protein interaction with alpha-synuclein by NMR
• Grantee: Edson Crusca Junior
• Support Opportunities: Scholarships in Brazil - Post-Doctoral