Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins-Reference-Cited by-同舟云学术

Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins

Published:2017-12-07 Issue:50 Volume:56 Page:6565-6574
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

van Rosmalen Martijn¹,Krom Mike¹,Merkx Maarten¹^ORCID

Affiliation:

1. Laboratory of Chemical Biology and Institute for Complex Molecular Systems (ICMS), Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands

Funder

FP7 Ideas: European Research Council

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00902

Reference60 articles.

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3. Development of an optimized backbone of FRET biosensors for kinases and GTPases

4. Construction of a linker library with widely controllable flexibility for fusion protein design

5. scFv multimers of the anti-neuraminidase antibody NC10: length of the linker between VH and VL domains dictates precisely the transition between diabodies and triabodies

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