What question did this study set out to answer?

To identify the side-chain interactions that direct the pairing of sulfhydryl groups into native disulfide bridges during ribonuclease refolding.

June 1, 1962Journal of Biological ChemistryOpen Access

Side-chain Interactions Governing the Pairing of Half-cystine Residues in Ribonuclease

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Authors

EHEdgar HaberGeneral / Preventive / Lipids CAChristian B. AnfinsenNew York State Department of Health

Discussion

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Implication

In vitro study reveals spontaneous refolding and disulfide pairing in reduced ribonuclease, demonstrating that the native tertiary structure is thermodynamically the most stable configuration.

Key Points

To identify the side-chain interactions that direct the pairing of sulfhydryl groups into native disulfide bridges during ribonuclease refolding.
Oxidized fully reduced ribonuclease containing eight sulfhydryl groups using molecular oxygen.
Conducted oxidation in the presence of reagents that perturb intramolecular bonding to generate non-native disulfide isomers.
Tested the capacity of enzymatically inactive isomeric derivatives to rearrange into the active native enzyme.
Oxidation of reduced ribonuclease recovered the native enzyme in nearly quantitative yields despite 105 possible four-disulfide pairing arrangements.
Perturbation of bonding produced inactive isomeric mixtures with physical properties similar to native ribonuclease.
Inactive disulfide isomers readily rearranged into the native enzyme, establishing that the native conformation is the thermodynamically most stable configuration.

Cite This Study

Haber et al. (1962) studied this question.

synapsesocial.com/papers/6a0a51805b6facdebcb4e73f https://doi.org/10.1016/s0021-9258(19)73945-3

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June 1, 1962Journal of Biological ChemistryOpen Access

Side-chain Interactions Governing the Pairing of Half-cystine Residues in Ribonuclease

View Full Paper

Ask AI

Bookmark

Authors

EHEdgar HaberGeneral / Preventive / Lipids CAChristian B. AnfinsenNew York State Department of Health

Discussion

Member takes

Implication

In vitro study reveals spontaneous refolding and disulfide pairing in reduced ribonuclease, demonstrating that the native tertiary structure is thermodynamically the most stable configuration.

Key Points

To identify the side-chain interactions that direct the pairing of sulfhydryl groups into native disulfide bridges during ribonuclease refolding.
Oxidized fully reduced ribonuclease containing eight sulfhydryl groups using molecular oxygen.
Conducted oxidation in the presence of reagents that perturb intramolecular bonding to generate non-native disulfide isomers.
Tested the capacity of enzymatically inactive isomeric derivatives to rearrange into the active native enzyme.
Oxidation of reduced ribonuclease recovered the native enzyme in nearly quantitative yields despite 105 possible four-disulfide pairing arrangements.
Perturbation of bonding produced inactive isomeric mixtures with physical properties similar to native ribonuclease.
Inactive disulfide isomers readily rearranged into the native enzyme, establishing that the native conformation is the thermodynamically most stable configuration.

Cite This Study

Haber et al. (1962) studied this question.

synapsesocial.com/papers/6a0a51805b6facdebcb4e73f https://doi.org/10.1016/s0021-9258(19)73945-3

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