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[Internal movement within globular proteins in accordance with the relationship between temperature and spin-lattice relaxation time].

S. I. Aksenov, Anton V. Filatov

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Abstract

The minima on the temperature dependence of T1 for protein protons were observed in dried SA at temperature about -100 degrees C and also about 0 degree C in SA and RNAase solutions in D2O. The minima of the temperature dependence were ascribed to motions of methyl groups of proteins, in the first case, and to oscillation of the polypeptide chain in the second case, both at characteristic frequencies of 10(8) s-1 in the minimum points.

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The minima on the temperature dependence of T1 for protein protons were observed in dried SA at temperature about -100 degrees C and also about 0 degree C in SA and RNAase solutions in D2O. The minima of the temperature dependence were ascribed to motions of methyl groups of proteins, in the first case, and to oscillation of the polypeptide chain in the second case, both at characteristic frequencies of 10(8) s-1 in the minimum points.

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Available abstract

The minima on the temperature dependence of T1 for protein protons were observed in dried SA at temperature about -100 degrees C and also about 0 degree C in SA and RNAase solutions in D2O. The minima of the temperature dependence were ascribed to motions of methyl groups of proteins, in the first case, and to oscillation of the polypeptide chain in the second case, both at characteristic frequencies of 10(8) s-1 in the minimum points.

Key concepts: Globular protein, Polypeptide chain, Maxima and minima, Oscillation (cell signaling), Relaxation (psychology), Lattice (music), Degree (music), Chemistry

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[Internal movement within globular proteins in accordance with the relationship between temperature and spin-lattice relaxation time]. — Research Paper | ScholarLens