A high-throughput workflow to analyze sequence-conformation relationships and explore hydrophobic patterning in disordered peptoids-Reference-Cited by-同舟云学术

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A high-throughput workflow to analyze sequence-conformation relationships and explore hydrophobic patterning in disordered peptoids

Published:2024-09 Issue: Volume: Page:
ISSN:2451-9294
Container-title:Chem
language:en
Short-container-title:Chem

Author:

Day Erin C.,Chittari Supraja S.,Cunha Keila C.,Zhao Roy J.,Dodds James N.,Davis Delaney C.,Baker Erin S.,Berlow Rebecca B.,Shea Joan-Emma,Kulkarni Rishikesh U.,Knight Abigail S.^ORCID

Funder

National Science Foundation

Air Force Office of Scientific Research

National Cancer Institute

NINDS

American Society for Engineering Education National Defense Science and Engineering Graduate Fellowship

NICHD

US Environmental Protection Agency

National Institute of Environmental Health Sciences

US Department of Energy

National Institute of General Medical Sciences

Publisher

Elsevier BV

Reference77 articles.

1. Studies on the Reduction and Re-Formation of Protein Disulfide Bonds;Anfinsen;J. Biol. Chem.,1961

2. Protein Structure in Relation to Function and Biosynthesis;Anfinsen,1956

3. Classification of Intrinsically Disordered Regions and Proteins;Van Der Lee;Chem. Rev.,2014

4. Tunable Biomaterials from Synthetic, Sequence-Controlled Polymers;Austin;Biomater. Sci.,2019

5. 100th Anniversary of Macromolecular Science Viewpoint: Opportunities in the Physics of Sequence-Defined Polymers;Perry;ACS Macro Lett.,2020

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