Surface salt bridges contribute to the extreme thermal stability of an FN3 ‐like domain from a thermophilic bacterium-Reference-Cited by-同舟云学术

Surface salt bridges contribute to the extreme thermal stability of an FN3 ‐like domain from a thermophilic bacterium

Published:2021-10-11 Issue:1 Volume:90 Page:270-281
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Boucher Lauren¹,Somani Sandeep¹^ORCID,Negron Christopher²,Ma Wenting¹,Jacobs Steven¹,Chan Winnie¹,Malia Thomas¹,Obmolova Galina¹,Teplyakov Alexey¹,Gilliland Gary L.¹,Luo Jinquan¹

Affiliation:

1. Janssen Research & Development, LLC Spring House Pennsylvania USA

2. Schrodinger Inc. New York New York USA

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26218

Reference69 articles.

1. Knottins: disulfide-bonded therapeutic and diagnostic peptides

2. Selection of high-affinity Centyrin FN3 domains from a simple library diversified at a combination of strand and loop positions

3. Non-immunoglobulin scaffolds: a focus on their targets

4. Design of novel FN3 domains with high stability by a consensus sequence approach

5. Adnectins: engineered target-binding protein therapeutics

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