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Related Concept Videos

Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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Amyloid Fibrils03:03

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Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Related Experiment Video

Updated: Jun 26, 2026

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Peptide processing and biology in human disease.

Suzana Kovac1, Arthur Shulkes, Graham S Baldwin

  • 1University of Melbourne, Department of Surgery, Austin Health, Heidelberg, Victoria, Australia.

Current Opinion in Endocrinology, Diabetes, and Obesity
|December 24, 2008
PubMed
Summary

Recent advances reveal gastrointestinal prohormones are bioactive, with mutations in processing enzymes linked to human diseases. Understanding precursor activity offers new therapeutic targets.

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Last Updated: Jun 26, 2026

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Published on: August 28, 2016

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Genetics

Background:

  • Gastrointestinal hormones regulate digestion and metabolism.
  • Hormone processing involves enzymatic cleavage of precursor proteins.
  • Mutations in processing enzymes can lead to disease.

Purpose of the Study:

  • To review recent advancements in gastrointestinal hormone processing.
  • To explore the impact of mutations in processing enzymes on human diseases.

Main Methods:

  • Literature review of recent studies on gastrointestinal hormone processing.
  • Analysis of human mutational data and mouse knockout models.
  • Examination of the bioactivity of hormone precursors.

Main Results:

  • Gastrointestinal prohormones for gastrin and gastrin-releasing peptide are bioactive.
  • Prohormones signal through different receptors than mature hormones.
  • Mutations in prohormone convertases are linked to various human pathophysiological conditions.

Conclusions:

  • Enzymes processing gastrointestinal hormones are crucial for mammalian biology.
  • Increased precursor concentrations, not just defective mature hormone production, contribute to symptoms.
  • Precursor-selective antagonists represent a potential therapeutic strategy.