Arginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions-Reference-Cited by-同舟云学术

Arginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions

Published:2019-07-17 Issue:32 Volume:58 Page:3413-3421
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Austerberry James I.¹²,Thistlethwaite Angela¹,Fisher Karl²,Golovanov Alexander P.²³^ORCID,Pluen Alain⁴,Esfandiary Reza⁵^ORCID,van der Walle Christopher F.⁶^ORCID,Warwicker Jim²³,Derrick Jeremy P.¹^ORCID,Curtis Robin²⁷^ORCID

Affiliation:

1. Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, United Kingdom

2. Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, United Kingdom

3. School of Chemistry, University of Manchester, Manchester M1 7DN, United Kingdom

4. Manchester Pharmacy School, University of Manchester, Manchester M13 9PL, United Kingdom

5. Dosage Form Design & Development, AstraZeneca, Gaithersburg, Maryland 20878, United States

6. Dosage Form Design & Development, AstraZeneca, Granta Park, Cambridge CB21 6GH, United Kingdom

7. School of Chemical Engineering and Analytical Science, University of Manchester, Manchester M1 7DN, United Kingdom

Funder

AstraZeneca

Biotechnology and Biological Sciences Research Council

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00367

Reference76 articles.

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5. A Lumry−Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding

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