Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

Balcı, Gülten Kavak

doi:10.1007/s10953-021-01052-z

Cited by 2 publications

(1 citation statement)

References 28 publications

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“…Both populations undergo some exchange [30]. These relaxation methods to examine water are still popular for measuring water-protein interactions across a wide range of different proteins, including lysozyme [31], keratin hydrogels [32], serum albumins [33,34] and soya protein [35].…”

Section: Introductionmentioning

confidence: 99%

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times

Molisso

Ces

Rowlands

et al. 2021

J. R. Soc. Interface.

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The interactions between small molecules and keratins are poorly understood. In this paper, a nuclear magnetic resonance method is presented to measure changes in the 1 H T 1 relaxation times of small molecules in human hair keratin to quantify their interaction with the fibre. Two populations of small-molecule compounds were identified with distinct relaxation times, demonstrating the partitioning of the compounds into different keratin environments. The changes in relaxation time for solvent in hair compared with bulk solvent were shown to be related to the molecular weight (MW) and the partition coefficient, LogP, of the solvent investigated. Compounds with low MWs and high hydrophilicities had greater reductions in their T 1 relaxation times and therefore experienced increased interactions with the hair fibre. The relative population sizes were also calculated. This is a significant step towards modelling the behaviour of small molecules in keratinous materials and other large insoluble fibrous proteins.

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Section: Introductionmentioning

confidence: 99%

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times

Molisso

Ces

Rowlands

et al. 2021

J. R. Soc. Interface.

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Application of nuclear magnetic resonance/magnetic resonance imaging techniques to estimate proton relaxation parameters at earth field

Ovalıoğlu

2022

Emerging Materials Research

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The nuclear magnetic resonance (NMR) field of earth may be utilized to estimate proton relaxation parameters in different liquids. In liquid samples, it can quantified proton relaxation durations T 1 and T 2 , along with the self-diffusion coefficient D, thanks to the magnetic field of the Earth. It was proved that it is feasible to distinguish between liquids based only on these characteristics by analyzing a wide range of liquid samples. In this paper, it was investigated whether it is possible to utilize Earth’s magnetic field Nuclear Magnetic Resonance (EFNMR) so as to correctly and practically quantify T 1 and T 2 along with the self-diffusion coefficient D. These findings pave the way for additional research into the use of EFNMR for the determination of relaxation parameters. It was acquired two-dimensional 1H NMR images of 50 ml of toluene solvent at low frequencies using the magnetic field of the Earth.

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Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

Cited by 2 publications

References 28 publications

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times

Application of nuclear magnetic resonance/magnetic resonance imaging techniques to estimate proton relaxation parameters at earth field

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Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

Cited by 2 publications

References 28 publications

Molecular interaction and partitioning in α-keratin using 1 H NMR spin-lattice ( T 1 ) relaxation times

Molecular interaction and partitioning in α-keratin using 1 H NMR spin-lattice ( T 1 ) relaxation times

Application of nuclear magnetic resonance/magnetic resonance imaging techniques to estimate proton relaxation parameters at earth field

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Product

Resources

About

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times

Molecular interaction and partitioning in α-keratin using ¹ H NMR spin-lattice ( T ₁ ) relaxation times