Site-Specific Phosphorylation of PDZ Domains

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Standard

Site-Specific Phosphorylation of PDZ Domains. / Ma, Sana; Strømgaard, Kristian; Clemmensen, Louise S.

Expressed Protein Ligation: Methods and Protocols. red. / Miquel Vila-Perelló. Humana Press, 2020. s. 235-261 (Methods in molecular biology (Clifton, N.J.), Bind 2133).

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Harvard

Ma, S, Strømgaard, K & Clemmensen, LS 2020, Site-Specific Phosphorylation of PDZ Domains. i MV-P (red.), Expressed Protein Ligation: Methods and Protocols. Humana Press, Methods in molecular biology (Clifton, N.J.), bind 2133, s. 235-261. https://doi.org/10.1007/978-1-0716-0434-2_12

APA

Ma, S., Strømgaard, K., & Clemmensen, L. S. (2020). Site-Specific Phosphorylation of PDZ Domains. I M. V-P. (red.), Expressed Protein Ligation: Methods and Protocols (s. 235-261). Humana Press. Methods in molecular biology (Clifton, N.J.) Bind 2133 https://doi.org/10.1007/978-1-0716-0434-2_12

Vancouver

Ma S, Strømgaard K, Clemmensen LS. Site-Specific Phosphorylation of PDZ Domains. I MV-P, red., Expressed Protein Ligation: Methods and Protocols. Humana Press. 2020. s. 235-261. (Methods in molecular biology (Clifton, N.J.), Bind 2133). https://doi.org/10.1007/978-1-0716-0434-2_12

Author

Ma, Sana ; Strømgaard, Kristian ; Clemmensen, Louise S. / Site-Specific Phosphorylation of PDZ Domains. Expressed Protein Ligation: Methods and Protocols. red. / Miquel Vila-Perelló. Humana Press, 2020. s. 235-261 (Methods in molecular biology (Clifton, N.J.), Bind 2133).

Bibtex

@inbook{6cc2d7cb75234854b936b55c15786739,

title = "Site-Specific Phosphorylation of PDZ Domains",

abstract = "Classical approaches for probing protein phosphorylation events rely on phosphomimicking amino acids or enzymatic phosphorylation of proteins. In many cases, phosphomimicking amino acids inadequately imitate actual protein phosphorylation, whereas the latter method suffers from an inability to control site specificity and stoichiometry. To circumvent these shortcomings, chemical biological approaches have been developed to enable introduction of phosphorylated amino acids into proteins in a reliable and controlled way. Here, we describe methods to make semisynthetic, phosphorylated PDZ domains, covering expressed protein ligation (EPL) strategies involving modifications within the N-terminal or C-terminal regions. We also enclose protocols for the biophysical characterization of the semisynthetic phosphorylated PDZ domains to establish whether the introduced phosphorylation affects protein structure, stability, and function.",

author = "Sana Ma and Kristian Str{\o}mgaard and Clemmensen, {Louise S}",

year = "2020",

doi = "10.1007/978-1-0716-0434-2_12",

language = "English",

isbn = "978-1-0716-0433-5",

series = "Methods in molecular biology (Clifton, N.J.)",

publisher = "Humana Press",

pages = "235--261",

editor = "{Miquel Vila-Perell{\'o}}",

booktitle = "Expressed Protein Ligation",

address = "United States",

}

RIS

TY - CHAP

T1 - Site-Specific Phosphorylation of PDZ Domains

AU - Ma, Sana

AU - Strømgaard, Kristian

AU - Clemmensen, Louise S

PY - 2020

Y1 - 2020

N2 - Classical approaches for probing protein phosphorylation events rely on phosphomimicking amino acids or enzymatic phosphorylation of proteins. In many cases, phosphomimicking amino acids inadequately imitate actual protein phosphorylation, whereas the latter method suffers from an inability to control site specificity and stoichiometry. To circumvent these shortcomings, chemical biological approaches have been developed to enable introduction of phosphorylated amino acids into proteins in a reliable and controlled way. Here, we describe methods to make semisynthetic, phosphorylated PDZ domains, covering expressed protein ligation (EPL) strategies involving modifications within the N-terminal or C-terminal regions. We also enclose protocols for the biophysical characterization of the semisynthetic phosphorylated PDZ domains to establish whether the introduced phosphorylation affects protein structure, stability, and function.

AB - Classical approaches for probing protein phosphorylation events rely on phosphomimicking amino acids or enzymatic phosphorylation of proteins. In many cases, phosphomimicking amino acids inadequately imitate actual protein phosphorylation, whereas the latter method suffers from an inability to control site specificity and stoichiometry. To circumvent these shortcomings, chemical biological approaches have been developed to enable introduction of phosphorylated amino acids into proteins in a reliable and controlled way. Here, we describe methods to make semisynthetic, phosphorylated PDZ domains, covering expressed protein ligation (EPL) strategies involving modifications within the N-terminal or C-terminal regions. We also enclose protocols for the biophysical characterization of the semisynthetic phosphorylated PDZ domains to establish whether the introduced phosphorylation affects protein structure, stability, and function.

U2 - 10.1007/978-1-0716-0434-2_12

DO - 10.1007/978-1-0716-0434-2_12

M3 - Book chapter

C2 - 32144671

SN - 978-1-0716-0433-5

T3 - Methods in molecular biology (Clifton, N.J.)

SP - 235

EP - 261

BT - Expressed Protein Ligation

A2 - null, Miquel Vila-Perelló

PB - Humana Press

ER -

ID: 269723160