Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Joseph W. Schafer"'
Autor:
Devlina Chakravarty, Joseph W. Schafer, Ethan A. Chen, Joseph F. Thole, Leslie A. Ronish, Myeongsang Lee, Lauren L. Porter
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Recent work suggests that AlphaFold (AF)–a deep learning-based model that can accurately infer protein structure from sequence–may discern important features of folded protein energy landscapes, defined by the diversity and frequency of
Externí odkaz:
https://doaj.org/article/7b3f673b8890490baeb8156a9bc56344
Autor:
Joseph W. Schafer, Lauren L. Porter
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract Although most globular proteins fold into a single stable structure, an increasing number have been shown to remodel their secondary and tertiary structures in response to cellular stimuli. State-of-the-art algorithms predict that these fold
Externí odkaz:
https://doaj.org/article/053ef8ad0dc9465398399847ee92fb80
Publikováno v:
Protein Science. 32
Publikováno v:
ACS Catal
Creating efficient and stable enzymes for catalysis in pharmaceutical and industrial laboratories is an important research goal. Arnold et al. used directed evolution to engineer a natural tryptophan synthase to create a mutant that is operable under
Autor:
Joseph W. Schafer, Steven D. Schwartz
Publikováno v:
ACS Catal
Protein engineering is a growing field with a variety of experimental techniques available for altering protein function. However, creating an enzyme de novo is still in its infancy, so far yielding enzymes of modest catalytic efficiency. In this stu
Autor:
Lauren L. Porter, Joseph W. Schafer, Devlina Chakravarty, Allen Kim, Swechha Rimal, Loren Looger, Ananya K. Majumdar, Mary Starich, Marie-Paule Strub
Publikováno v:
Biophysical Journal. 122:470a
Publikováno v:
Biophysical Journal. 118:138a-139a
Publikováno v:
J Am Chem Soc
The design of artificial enzymes is an emerging field of research. Although progress has been made, the catalytic proficiency of many designed enzymes is low compared to natural enzymes. Nevertheless, recently Hilvert et al. ( Nat. Chem. 2017, 9, 50-
Publikováno v:
Biophysical Journal. 116:432a