Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior

Carlos A. Castañeda; Liat Spasser; Sudhir N. Bavikar; Ashraf Brik; David Fushman

doi:10.1002/anie.201104649

Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior

Carlos A. Castañeda
, Liat Spasser
, Sudhir N. Bavikar
, Ashraf Brik
, David Fushman

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

"Seeing" each monomer in ubiquitin chains: By combination of the chemical synthesis of one ubiquitin monomer with recombinant expression of its ¹⁵N-containing counterpart, the labeling of ubiquitins in non-enzymatically assembled di-ubiquitin chains was achieved, to enable monomer-specific studies in solution. This allowed the first characterization of the structure, dynamics, intrachain interactions, and ligand binding of Lys33-linked di-ubiquitin.

Original language	English
Pages (from-to)	11210-11214
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	47
DOIs	https://doi.org/10.1002/anie.201104649
State	Published - 18 Nov 2011

Keywords

chain structures
isotopic labeling
protein structures
semisynthesis
ubiquitin

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201104649

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AU - Castañeda, Carlos A.

AU - Spasser, Liat

AU - Bavikar, Sudhir N.

AU - Brik, Ashraf

AU - Fushman, David

PY - 2011/11/18

Y1 - 2011/11/18

N2 - "Seeing" each monomer in ubiquitin chains: By combination of the chemical synthesis of one ubiquitin monomer with recombinant expression of its 15N-containing counterpart, the labeling of ubiquitins in non-enzymatically assembled di-ubiquitin chains was achieved, to enable monomer-specific studies in solution. This allowed the first characterization of the structure, dynamics, intrachain interactions, and ligand binding of Lys33-linked di-ubiquitin.

AB - "Seeing" each monomer in ubiquitin chains: By combination of the chemical synthesis of one ubiquitin monomer with recombinant expression of its 15N-containing counterpart, the labeling of ubiquitins in non-enzymatically assembled di-ubiquitin chains was achieved, to enable monomer-specific studies in solution. This allowed the first characterization of the structure, dynamics, intrachain interactions, and ligand binding of Lys33-linked di-ubiquitin.

KW - chain structures

KW - isotopic labeling

KW - protein structures

KW - semisynthesis

KW - ubiquitin

UR - https://www.scopus.com/pages/publications/81255172803

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ER -

Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior

Abstract

Keywords

ASJC Scopus subject areas

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