The role of interchain disulphide bridges in the conformational stability of human immunoglobulin G1 subclass. Hydrogen deuterium exchange studies

S. Y. Venyaminov, E. Rajnavolgyi, G. A. Medgyesi, J. Gergely, P. Závodszky

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Abstract

The hydrogen deuterium exchange data of human immunoglobulin G1 (IgG1) are interpreted by assuming fast fluctuations of the protein conformation, through which the peptide groups become exposed to the solvent. The probability of solvent exposure of peptide hydrogens reflects a rather loose conformation for native IgG in comparison with other globular proteins. The probability of solvent exposure is greater than 10-3 for half of the peptide groups, which shows that the conformational transitions by which these groups are exposed to the solvent are accompanied by changes in standard free energy less than 17 kJ/mol (4 kcal/mol). In the range of pH 6.2-8.45, at 25°C no gross conformational changes are reflected in the hydrogen deuterium exchange behaviour of the native, the reduced nonalkylated reassociated and the reduced S alkylated reassociated IgG1. No difference could be detected in the conformational stability of the native and reoxidised reassociated IgG1 proteins. The lack of inter subunit disulphide bridges in S alkylated reassociated molecules results in an increased conformational motility. This destabilization of protein conformation affects about 90% of the peptide groups covered by the measurements, and corresponds to changes in standard free energy of 8 kJ/mol on the average.

Original languageEnglish
Pages (from-to)81-86
Number of pages6
JournalEuropean Journal of Biochemistry
Volume67
Issue number1
DOIs
Publication statusPublished - 1976

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Deuterium
Disulfides
Immunoglobulins
Hydrogen
Conformations
Peptides
Protein Conformation
Free energy
Proteins
Electronic data interchange
Immunoglobulin G
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "The role of interchain disulphide bridges in the conformational stability of human immunoglobulin G1 subclass. Hydrogen deuterium exchange studies",
abstract = "The hydrogen deuterium exchange data of human immunoglobulin G1 (IgG1) are interpreted by assuming fast fluctuations of the protein conformation, through which the peptide groups become exposed to the solvent. The probability of solvent exposure of peptide hydrogens reflects a rather loose conformation for native IgG in comparison with other globular proteins. The probability of solvent exposure is greater than 10-3 for half of the peptide groups, which shows that the conformational transitions by which these groups are exposed to the solvent are accompanied by changes in standard free energy less than 17 kJ/mol (4 kcal/mol). In the range of pH 6.2-8.45, at 25°C no gross conformational changes are reflected in the hydrogen deuterium exchange behaviour of the native, the reduced nonalkylated reassociated and the reduced S alkylated reassociated IgG1. No difference could be detected in the conformational stability of the native and reoxidised reassociated IgG1 proteins. The lack of inter subunit disulphide bridges in S alkylated reassociated molecules results in an increased conformational motility. This destabilization of protein conformation affects about 90{\%} of the peptide groups covered by the measurements, and corresponds to changes in standard free energy of 8 kJ/mol on the average.",
author = "Venyaminov, {S. Y.} and E. Rajnavolgyi and Medgyesi, {G. A.} and J. Gergely and P. Z{\'a}vodszky",
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T1 - The role of interchain disulphide bridges in the conformational stability of human immunoglobulin G1 subclass. Hydrogen deuterium exchange studies

AU - Venyaminov, S. Y.

AU - Rajnavolgyi, E.

AU - Medgyesi, G. A.

AU - Gergely, J.

AU - Závodszky, P.

PY - 1976

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N2 - The hydrogen deuterium exchange data of human immunoglobulin G1 (IgG1) are interpreted by assuming fast fluctuations of the protein conformation, through which the peptide groups become exposed to the solvent. The probability of solvent exposure of peptide hydrogens reflects a rather loose conformation for native IgG in comparison with other globular proteins. The probability of solvent exposure is greater than 10-3 for half of the peptide groups, which shows that the conformational transitions by which these groups are exposed to the solvent are accompanied by changes in standard free energy less than 17 kJ/mol (4 kcal/mol). In the range of pH 6.2-8.45, at 25°C no gross conformational changes are reflected in the hydrogen deuterium exchange behaviour of the native, the reduced nonalkylated reassociated and the reduced S alkylated reassociated IgG1. No difference could be detected in the conformational stability of the native and reoxidised reassociated IgG1 proteins. The lack of inter subunit disulphide bridges in S alkylated reassociated molecules results in an increased conformational motility. This destabilization of protein conformation affects about 90% of the peptide groups covered by the measurements, and corresponds to changes in standard free energy of 8 kJ/mol on the average.

AB - The hydrogen deuterium exchange data of human immunoglobulin G1 (IgG1) are interpreted by assuming fast fluctuations of the protein conformation, through which the peptide groups become exposed to the solvent. The probability of solvent exposure of peptide hydrogens reflects a rather loose conformation for native IgG in comparison with other globular proteins. The probability of solvent exposure is greater than 10-3 for half of the peptide groups, which shows that the conformational transitions by which these groups are exposed to the solvent are accompanied by changes in standard free energy less than 17 kJ/mol (4 kcal/mol). In the range of pH 6.2-8.45, at 25°C no gross conformational changes are reflected in the hydrogen deuterium exchange behaviour of the native, the reduced nonalkylated reassociated and the reduced S alkylated reassociated IgG1. No difference could be detected in the conformational stability of the native and reoxidised reassociated IgG1 proteins. The lack of inter subunit disulphide bridges in S alkylated reassociated molecules results in an increased conformational motility. This destabilization of protein conformation affects about 90% of the peptide groups covered by the measurements, and corresponds to changes in standard free energy of 8 kJ/mol on the average.

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