Výsledky vyhledávání - "Jennifer H. Yoon"

Nine-Residue Peptide Self-Assembles in the Presence of Silver to Produce a Self-Healing, Cytocompatible, Antimicrobial Hydrogel

Autor: Mary Beth B. Monroe, Kelly M. Schultz, Olga V. Makhlynets, Zsofia Lengyel-Zhand, Matthew D. Wehrman, Areetha D'Souza, Alex Sternisha, Liam R. Marshall, Pallavi M. Gosavi, Jennifer H. Yoon, Garrick Centola, Henry T. Beaman

Publikováno v: ACS Applied Materials & Interfaces. 12:17091-17099

Silver compounds have been used extensively for wound healing because of their antimicrobial properties, but high concentrations of silver are toxic to mammalian cells. We designed a peptide that binds silver and releases only small amounts of this i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cffc8b2a3774191bce25330733394c7
https://doi.org/10.1021/acsami.0c01154

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Mechanistic studies of the cofactor assembly in class Ib ribonucleotide reductases and protein affinity for MnII and FeII

Autor: Denis Cipurko, Olga V. Makhlynets, Jacky Wu, Megha Jayachandran, Joyce Quon, Jennifer H. Yoon

Publikováno v: Metallomics. 13

Ribonucleotide reductase (RNR) is an essential enzyme found in all organisms. The function of RNR is to catalyze the conversion of nucleotides to deoxynucleotides. RNRs rely on metallocofactors to oxidize a conserved cysteine in the active site of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2de8dbfb0812e292b7392b66a10cbef
https://doi.org/10.1093/mtomcs/mfab062

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Uno Ferro, a de novo designed protein, binds transition metals with high affinity and stabilizes semiquinone radical anion

Autor: Olga V. Makhlynets, Areetha D'Souza, Elizabeth R. Caselle, Alona Kulesha, Alexander N. Volkov, Joel J. L. Rempillo, Christos Costeas, Zsofia Lengyel-Zhand, Jennifer H. Yoon, Cara Chester

Publikováno v: Chemistry

Metalloenzymes often utilize radicals in order to facilitate chemical reactions. Recently, DeGrado and coworkers have discovered that model proteins can efficiently stabilize semiquinone radical anion produced by oxidation of 3,5-di-tert-butylcatecho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33339bf8969ed07dd5ec2392c26ee450
https://europepmc.org/articles/PMC6891133/

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Kemp Eliminases of the AlleyCat Family Possess High Substrate Promiscuity

Autor: Areetha D'Souza, Elizabeth A. Caselle, Olga V. Makhlynets, Yurii S. Moroz, Alexander N. Volkov, Ivan V. Korendovych, Carlos A. Castañeda, Marcello Forconi, Zsófia Lengyel, Patricia L. Tolbert, Jennifer H. Yoon, Joel J. L. Rempillo, Sagar Bhattacharya

Minimalist enzymes designed to catalyze model reactions provide useful starting points for creating catalysts for practically important chemical transformations. We have shown that Kemp eliminases of the AlleyCat family facilitate conversion of leflu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fc2e2a0538e3e26909b77ec5f139b12
https://europepmc.org/articles/PMC6884320/

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Contributions of primary coordination ligands and importance of outer sphere interactions in UFsc, a de novo designed protein with high affinity for metal ions

Autor: Alona Kulesha, Jennifer H. Yoon, Areetha D'Souza, Olga V. Makhlynets, Cara Chester, Christos Costeas

Publikováno v: Journal of Inorganic Biochemistry. 212:111224

Metalloproteins constitute nearly half of all proteins and catalyze some of the most complex chemical reactions. Recently, we reported a design of 4G-UFsc (Uno Ferro single chain), a single chain four-helical bundle with extraordinarily high (30 pM)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::040fe6209c03061815cd23e0bf8641d7
https://doi.org/10.1016/j.jinorgbio.2020.111224

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New Tricks for Old Proteins: Single Mutations in a Nonenzymatic Protein Give Rise to Various Enzymatic Activities

Autor: Olga V. Makhlynets, Pallavi M. Gosavi, Tiffany T. Dunston, Ivan V. Korendovych, Yibing Wu, Nico A. J. van Nuland, Jennifer H. Yoon, Alissa B. Olsen, Korrie L. Mack, Olesia V. Moroz, Jaclyn M. McLaughlin, Yurii S. Moroz

Publikováno v: Journal of the American Chemical Society. 137:14905-14911

Design of a new catalytic function in proteins, apart from its inherent practical value, is important for fundamental understanding of enzymatic activity. Using a computationally inexpensive, minimalistic approach that focuses on introducing a single

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f8203af4f16df199d2c88946c896999
https://doi.org/10.1021/jacs.5b07812

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Design of an allosterically regulated retroaldolase

Autor: Jennifer H. Yoon, Elizabeth A. Raymond, Korrie L. Mack, Yurii S. Moroz, Ivan V. Korendovych, Olesia V. Moroz

Publikováno v: Protein Science. 24:561-570

We employed a minimalist approach for design of an allosterically controlled retroaldo- lase. Introduction of a single lysine residue into the nonenzymatic protein calmodulin led to a 15,000-fold increase in the second order rate constant for retroal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::075036804624b6075b00b4f078ea5677
https://doi.org/10.1002/pro.2622

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