Understanding and applications of Ser/Gly linkers in protein engineering

Eric Ceballos-Alcantarilla, Maarten Merkx

Onderzoeksoutput: Hoofdstuk in Boek/Rapport/CongresprocedureHoofdstukAcademicpeer review

Samenvatting

Peptide linkers consisting of repeats of glycine and serine residues are commonly chosen by protein engineers to introduce flexible and hydrophilic spacers between protein domains. Given the popularity of these linkers, gaining a quantitative insight in their conformational behavior is important to understand the effect on functional properties of fusion proteins, including energy transfer efficiency in luminescent sensor proteins, intramolecular domain interactions and (multivalent) binding. In this chapter, we discuss how the conformational behavior of Ser/Gly linkers can be described using random coil models, and how measuring FRET as a function of linker length can be used to obtain empirical values for the stiffness of linkers containing different Ser-to-Gly ratios. Subsequently, we show how these models and the experimentally determined linker stiffness can be used to explain and predict the functional properties of multidomain proteins, providing useful rules-of-thumb and design tools for optimal linker engineering.

Originele taal-2Engels
TitelLinkers in Biomacromolecules
RedacteurenMaarten Merkx
UitgeverijAcademic Press Inc.
Pagina's1-22
Aantal pagina's22
ISBN van geprinte versie9780128208182
DOI's
StatusGepubliceerd - jan 2021

Publicatie series

NaamMethods in Enzymology
Volume647
ISSN van geprinte versie0076-6879
ISSN van elektronische versie1557-7988

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