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

Harvard

Safavi-Hemami, H, Foged, MM & Ellgaard, L 2018, Evolutionary Adaptations to Cysteine-rich Peptide Folding. i MJ Feige (red.), Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering . Royal Society of Chemistry, Chemical Biology, bind 9, s. 99-128. https://doi.org/10.1039/9781788013253

APA

Safavi-Hemami, H., Foged, M. M., & Ellgaard, L. (2018). Evolutionary Adaptations to Cysteine-rich Peptide Folding. I M. J. Feige (red.), Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering (s. 99-128). Royal Society of Chemistry. Chemical Biology Bind 9 https://doi.org/10.1039/9781788013253

Vancouver

Safavi-Hemami H, Foged MM, Ellgaard L. Evolutionary Adaptations to Cysteine-rich Peptide Folding. I Feige MJ, red., Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering . Royal Society of Chemistry. 2018. s. 99-128. (Chemical Biology, Bind 9). https://doi.org/10.1039/9781788013253

Author

Safavi-Hemami, Helena ; Foged, Mads Møller ; Ellgaard, Lars. / Evolutionary Adaptations to Cysteine-rich Peptide Folding. 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).

Bibtex

@inbook{d40a9a0d82b44ab0ac5816534af92e75,
title = "Evolutionary Adaptations to Cysteine-rich Peptide Folding",
abstract = "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.",
author = "Helena Safavi-Hemami and Foged, {Mads M{\o}ller} and Lars Ellgaard",
year = "2018",
doi = "10.1039/9781788013253",
language = "English",
isbn = "978-1-78262-990-0",
series = "Chemical Biology",
publisher = "Royal Society of Chemistry",
pages = "99--128",
editor = "Feige, {Matthias J.}",
booktitle = "Oxidative Folding of Proteins",
address = "United Kingdom",

}

RIS

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