Evolutionary Adaptations to Cysteine-rich Peptide Folding
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Evolutionary Adaptations to Cysteine-rich Peptide Folding. / Safavi-Hemami, Helena; Foged, Mads Møller; Ellgaard, Lars.
Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering . red. / Matthias J. Feige. Royal Society of Chemistry, 2018. s. 99-128 (Chemical Biology, Bind 9).Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt
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TY - CHAP
T1 - Evolutionary Adaptations to Cysteine-rich Peptide Folding
AU - Safavi-Hemami, Helena
AU - Foged, Mads Møller
AU - Ellgaard, Lars
PY - 2018
Y1 - 2018
N2 - Cysteine-rich peptides are highly abundant in nature, and provide a fascinating insight into protein folding, structure, chemical modification and function. The largest number and diversity of cysteine-rich peptides are produced by organisms at the interface between predator and prey, and host and pathogen (or symbiont). The small peptides produced by these organisms are characterized by hypervariable sequences interspersed with conserved cysteines involved in disulfide bond formation, and include some of the fastest evolving genes in nature. The diversity of structural scaffolds found for cysteine-rich peptides suggests that specialized adaptations have evolved to ensure their efficient folding and secretion in their producer organisms. This chapter uses conopeptides, neurotoxic peptides found in the venoms of predatory marine cone snails, as model systems to discuss some of these adaptations discovered in organisms that provide a rich source of cysteine-rich peptides with diverse structural scaffolds.
AB - Cysteine-rich peptides are highly abundant in nature, and provide a fascinating insight into protein folding, structure, chemical modification and function. The largest number and diversity of cysteine-rich peptides are produced by organisms at the interface between predator and prey, and host and pathogen (or symbiont). The small peptides produced by these organisms are characterized by hypervariable sequences interspersed with conserved cysteines involved in disulfide bond formation, and include some of the fastest evolving genes in nature. The diversity of structural scaffolds found for cysteine-rich peptides suggests that specialized adaptations have evolved to ensure their efficient folding and secretion in their producer organisms. This chapter uses conopeptides, neurotoxic peptides found in the venoms of predatory marine cone snails, as model systems to discuss some of these adaptations discovered in organisms that provide a rich source of cysteine-rich peptides with diverse structural scaffolds.
U2 - 10.1039/9781788013253
DO - 10.1039/9781788013253
M3 - Book chapter
SN - 978-1-78262-990-0
T3 - Chemical Biology
SP - 99
EP - 128
BT - Oxidative Folding of Proteins
A2 - Feige, Matthias J.
PB - Royal Society of Chemistry
ER -
ID: 200968051