DENATURATION OF PROTEINS. V. N.M.R. STUDY OF THE ARGININE RESIDUES OF LYSOZYME

J. H. Bradbury, Raymond S. Norton

Research output: Contribution to journalArticleResearchpeer-review

8 Citations (Scopus)

Abstract

The heat denaturation of lysozyme has been studied by proton magnetic resonance spectroscopy at 220 MHz in water at pH 2.8. At 20°C a broad resonance is observed at 6.8δ due to the arginine NH2 resonances, which becomes a well defined triple resonance at 40°C, without any change in the rest of the spectrum. This sharpening of the arginine NH2 resonances is due to their increased mobilities and/or some normalisation of their chemical shifts. It is proposed that the surface structure of lysozyme is loosened at 40°C, without any change in the hydrophobic core and this is considered to be an intermediate phase in its heat denaturation. The heat denatured product at 80°C in D2O retains some noncovalent interactions, since further treatment with guanidine deuterochloride or mercaptoethanol causes sharpening of the aromatic region of the spectrum.

Original languageEnglish
Pages (from-to)295-302
Number of pages8
JournalInternational Journal of Peptide and Protein Research
Volume6
Issue number5
DOIs
Publication statusPublished - 1974
Externally publishedYes

Cite this

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title = "DENATURATION OF PROTEINS. V. N.M.R. STUDY OF THE ARGININE RESIDUES OF LYSOZYME",
abstract = "The heat denaturation of lysozyme has been studied by proton magnetic resonance spectroscopy at 220 MHz in water at pH 2.8. At 20°C a broad resonance is observed at 6.8δ due to the arginine NH2 resonances, which becomes a well defined triple resonance at 40°C, without any change in the rest of the spectrum. This sharpening of the arginine NH2 resonances is due to their increased mobilities and/or some normalisation of their chemical shifts. It is proposed that the surface structure of lysozyme is loosened at 40°C, without any change in the hydrophobic core and this is considered to be an intermediate phase in its heat denaturation. The heat denatured product at 80°C in D2O retains some noncovalent interactions, since further treatment with guanidine deuterochloride or mercaptoethanol causes sharpening of the aromatic region of the spectrum.",
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DENATURATION OF PROTEINS. V. N.M.R. STUDY OF THE ARGININE RESIDUES OF LYSOZYME. / Bradbury, J. H.; Norton, Raymond S.

In: International Journal of Peptide and Protein Research, Vol. 6, No. 5, 1974, p. 295-302.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - DENATURATION OF PROTEINS. V. N.M.R. STUDY OF THE ARGININE RESIDUES OF LYSOZYME

AU - Bradbury, J. H.

AU - Norton, Raymond S.

PY - 1974

Y1 - 1974

N2 - The heat denaturation of lysozyme has been studied by proton magnetic resonance spectroscopy at 220 MHz in water at pH 2.8. At 20°C a broad resonance is observed at 6.8δ due to the arginine NH2 resonances, which becomes a well defined triple resonance at 40°C, without any change in the rest of the spectrum. This sharpening of the arginine NH2 resonances is due to their increased mobilities and/or some normalisation of their chemical shifts. It is proposed that the surface structure of lysozyme is loosened at 40°C, without any change in the hydrophobic core and this is considered to be an intermediate phase in its heat denaturation. The heat denatured product at 80°C in D2O retains some noncovalent interactions, since further treatment with guanidine deuterochloride or mercaptoethanol causes sharpening of the aromatic region of the spectrum.

AB - The heat denaturation of lysozyme has been studied by proton magnetic resonance spectroscopy at 220 MHz in water at pH 2.8. At 20°C a broad resonance is observed at 6.8δ due to the arginine NH2 resonances, which becomes a well defined triple resonance at 40°C, without any change in the rest of the spectrum. This sharpening of the arginine NH2 resonances is due to their increased mobilities and/or some normalisation of their chemical shifts. It is proposed that the surface structure of lysozyme is loosened at 40°C, without any change in the hydrophobic core and this is considered to be an intermediate phase in its heat denaturation. The heat denatured product at 80°C in D2O retains some noncovalent interactions, since further treatment with guanidine deuterochloride or mercaptoethanol causes sharpening of the aromatic region of the spectrum.

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