Understanding the interactions between protein stabilizers and the peptide bond through the analysis of the volumetric and compressibility properties for the model systems

Kaczkowska, Emilia; Wawer, Jarosław; Tyczyńska, Magdalena; Jóźwiak, Małgorzata; Krakowiak, Joanna

doi:10.1016/j.jct.2021.106485

Cited by 2 publications

(1 citation statement)

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“…N-Methylacetamide (NMA) is considered as a minimal part of the peptide backbone that contains a peptide linkage and, additionally, two hydrophobic methyl groups. Aqueous solutions of NMA in the presence of osmolytes have been studied mainly theoretically [14][15][16][17][18][19] and rarely experimentally [20][21][22], and they have provided information about various interactions that play a role in the protein folding process.…”

Section: Introductionmentioning

confidence: 99%

Interactions in Ternary Aqueous Solutions of NMA and Osmolytes—PARAFAC Decomposition of FTIR Spectra Series

Kaczkowska

Panuszko

Bruździak

2021

IJMS

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Intermolecular interactions in aqueous solutions are crucial for virtually all processes in living cells. ATR-FTIR spectroscopy is a technique that allows changes caused by many types of such interactions to be registered; however, binary solutions are sometimes difficult to solve in these terms, while ternary solutions are even more difficult. Here, we present a method of data pretreatment that facilitates the use of the Parallel Factor Analysis (PARAFAC) decomposition of ternary solution spectra into parts that are easier to analyze. Systems of the NMA–water–osmolyte-type were used to test the method and to elucidate information on the interactions between N-Methylacetamide (NMA, a simple peptide model) with stabilizing (trimethylamine N-oxide, glycine, glycine betaine) and destabilizing osmolytes (n-butylurea and tetramethylurea). Systems that contain stabilizers change their vibrational structure to a lesser extent than those with denaturants. Changes in the latter are strong and can be related to the formation of direct NMA–destabilizer interactions.

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