Chemical Synthesis of PDZ Domains

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Chemical Synthesis of PDZ Domains. / Kossmann, Christin; Ma, Sana; Clemmensen, Louise S.; Strømgaard, Kristian.

Methods in Molecular Biology. ed. / Jean-Paul Borg. Humana Press, 2021. p. 193-216 (Methods in Molecular Biology, Vol. 2256).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Kossmann, C, Ma, S, Clemmensen, LS & Strømgaard, K 2021, Chemical Synthesis of PDZ Domains. in J-PB (ed.), Methods in Molecular Biology. Humana Press, Methods in Molecular Biology, vol. 2256, pp. 193-216. https://doi.org/10.1007/978-1-0716-1166-1_12

APA

Kossmann, C., Ma, S., Clemmensen, L. S., & Strømgaard, K. (2021). Chemical Synthesis of PDZ Domains. In J-P. B. (Ed.), Methods in Molecular Biology (pp. 193-216). Humana Press. Methods in Molecular Biology Vol. 2256 https://doi.org/10.1007/978-1-0716-1166-1_12

Vancouver

Kossmann C, Ma S, Clemmensen LS, Strømgaard K. Chemical Synthesis of PDZ Domains. In J-PB, editor, Methods in Molecular Biology. Humana Press. 2021. p. 193-216. (Methods in Molecular Biology, Vol. 2256). https://doi.org/10.1007/978-1-0716-1166-1_12

Author

Kossmann, Christin ; Ma, Sana ; Clemmensen, Louise S. ; Strømgaard, Kristian. / Chemical Synthesis of PDZ Domains. Methods in Molecular Biology. editor / Jean-Paul Borg. Humana Press, 2021. pp. 193-216 (Methods in Molecular Biology, Vol. 2256).

Bibtex

@inbook{5ed1822fdd67453dbe7476fc978f70a8,
title = "Chemical Synthesis of PDZ Domains",
abstract = "Developments in chemical protein synthesis have enabled the generation of tailor-made proteins including incorporation of many types of modifications into proteins, enhancing our ability to control site-specificity of protein posttranslational modifications (PTMs), modify protein backbones and introduce photocrosslinking probes. For PDZ (postsynaptic density protein, disks large, zonula occludens) protein domains, expressed protein ligation (EPL) has been employed to introduce analogs of cognate amino acids, amide-to-ester bond mutations, and phosphorylations in the study of PDZ domain-mediated protein-protein interactions (PPIs). Here, we present protocols for EPL of PDZ domains focusing on phosphorylation and amide-to-ester modifications in the PDZ domain proteins.",
keywords = "Amide-to-ester mutation, Expressed protein ligation, Native chemical ligation, Phosphorylation, Protein modification, Solid-phase peptide synthesis",
author = "Christin Kossmann and Sana Ma and Clemmensen, {Louise S.} and Kristian Str{\o}mgaard",
note = "Publisher Copyright: {\textcopyright} 2021, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2021",
doi = "10.1007/978-1-0716-1166-1_12",
language = "English",
isbn = "978-1-0716-1165-4",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "193--216",
editor = "{Jean-Paul Borg}",
booktitle = "Methods in Molecular Biology",
address = "United States",

}

RIS

TY - CHAP

T1 - Chemical Synthesis of PDZ Domains

AU - Kossmann, Christin

AU - Ma, Sana

AU - Clemmensen, Louise S.

AU - Strømgaard, Kristian

N1 - Publisher Copyright: © 2021, Springer Science+Business Media, LLC, part of Springer Nature.

PY - 2021

Y1 - 2021

N2 - Developments in chemical protein synthesis have enabled the generation of tailor-made proteins including incorporation of many types of modifications into proteins, enhancing our ability to control site-specificity of protein posttranslational modifications (PTMs), modify protein backbones and introduce photocrosslinking probes. For PDZ (postsynaptic density protein, disks large, zonula occludens) protein domains, expressed protein ligation (EPL) has been employed to introduce analogs of cognate amino acids, amide-to-ester bond mutations, and phosphorylations in the study of PDZ domain-mediated protein-protein interactions (PPIs). Here, we present protocols for EPL of PDZ domains focusing on phosphorylation and amide-to-ester modifications in the PDZ domain proteins.

AB - Developments in chemical protein synthesis have enabled the generation of tailor-made proteins including incorporation of many types of modifications into proteins, enhancing our ability to control site-specificity of protein posttranslational modifications (PTMs), modify protein backbones and introduce photocrosslinking probes. For PDZ (postsynaptic density protein, disks large, zonula occludens) protein domains, expressed protein ligation (EPL) has been employed to introduce analogs of cognate amino acids, amide-to-ester bond mutations, and phosphorylations in the study of PDZ domain-mediated protein-protein interactions (PPIs). Here, we present protocols for EPL of PDZ domains focusing on phosphorylation and amide-to-ester modifications in the PDZ domain proteins.

KW - Amide-to-ester mutation

KW - Expressed protein ligation

KW - Native chemical ligation

KW - Phosphorylation

KW - Protein modification

KW - Solid-phase peptide synthesis

U2 - 10.1007/978-1-0716-1166-1_12

DO - 10.1007/978-1-0716-1166-1_12

M3 - Book chapter

C2 - 34014524

AN - SCOPUS:85106412026

SN - 978-1-0716-1165-4

SN - 978-1-0716-1168-5

T3 - Methods in Molecular Biology

SP - 193

EP - 216

BT - Methods in Molecular Biology

A2 - null, Jean-Paul Borg

PB - Humana Press

ER -

ID: 273635447