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Book ChapterDOI

Peptide Bond Formation

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TLDR
This chapter discusses peptide bond formation and the bearing of new data and new discoveries on the problem of the enzymatic synthesis of protein.
Abstract
Publisher Summary This chapter discusses peptide bond formation. Peptide bonds may be broken and reconstituted by simple hydrolysis and its reversal by transferring reactions in which one of the participants need not be a peptide. Studies on the enzymatic synthesis of small peptides and quasi-peptides discovered examples on how free energy ultimately derived from respiration is used for peptide synthesis. A new field of investigation opened up by the finding that free amino acids are incorporated into protein by peptide linkages in the interior of the molecule. This reaction occurs in all living forms, and seen against the background of the apparent stability of protein in the cell, is remarkably rapid. The chapter discusses the bearing of these new data and new discoveries on the problem of the enzymatic synthesis of protein.

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Citations
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Book ChapterDOI

Synthesis and chemical properties of poly-alpha-amino acids.

TL;DR: The methods used to establish the chemical constitution of the polymers and their average molecular weights are given and the most suitable and commonly used are the N-carboxy-α-amino acid anhydrides.
Journal ArticleDOI

Stability of peptides in high-temperature aqueous solutions

TL;DR: In this paper, it was shown that peptides, polypeptides, and proteins may survive hydrothermal alteration of organic matter depending on the rates of the hydrolysis reactions.
References
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Journal ArticleDOI

Uptake of radioactive alanine in vitro into the proteins of rat liver fractions.

TL;DR: Preliminary experiments indicated that a correlation exists between uptake of the labeled amino acid into protein and oxidative phosphorylation and a synergistic action of two fractions is necessary in order that the label be incorporated.
Journal ArticleDOI

The free amino groups of haemoglobins.

TL;DR: It is recommended that the proteases described in this paper shall be considered identical until evidence to the contrary is adduced, and that they be called leaf proteases, adding where necessary the name of the plant.
Journal ArticleDOI

The specific esterase activity of trypsin.

TL;DR: In the course of an investigation of the inhibition of crystalline pancreatic proteolytic enzymes by specific low molecular weight compounds the discovery was made that crystalline trypsin is likewise a powerful catalyst for the hydrolysis of certain amino acid esters.
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