The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain.

By C. Anfinsen, E. Haber, M. Sela, F. H. White. 1961

In this article, Anfinsen, Haber, Sela, and White reported that there existed a considerable lag phase before enzymatic activity appeared after the sample of bovine pancreatic ribonuclease was treated with mercaptoethanol in urea, during which period the sulfhydrl titer and the specific optical rotation changed along a curve similar to that of a first-order reaction. The lag in enzymatic activity in vitro often took several hours, while the same process seemed to take only a few minutes in vivo. This discrepancy eventually led to the discovery of an enzyme system in the endoplasmic reticulum of cells that catalyzes the disulfide interchange reaction, and subsequently, the rapid formation of the correct, native disulfide pairing in relatively short order.

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Citations in the corpus

Evaluating Protein Transfer Learning with TAPE (2019, background): “Understanding how primary sequence folds into tertiary structure is a fundamental goal of biochemistry [2].”
NetSurfP-2.0: improved prediction of protein structural features by integrated deep learning (2018, methodology): “of a protein are encoded in its primary sequence alone, is more than 50 years old.(1) As a practical application of it, several methods have been developed over the last decades to predict from sequence only several protein structural features, including solvent accessibility, secondary structure, b”
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