Zobrazeno 1 - 10
of 43
pro vyhledávání: '"C. Baxa"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(20)
To import large metabolites across the outer membrane of gram-negative bacteria, TonB-dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the Escherichia coli vitamin B12 TBDT, TonB binds and cou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dd87f6c39e74faa0ba0a0dbfd9e698ad
https://pubmed.ncbi.nlm.nih.gov/35549554
https://pubmed.ncbi.nlm.nih.gov/35549554
To import large metabolites across the outer membrane of Gram-negative bacteria, TonB dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the E. coli vitamin B12 TBDT, TonB binds and couples BtuB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::158829da09b552be03d8d168efaffb63
https://doi.org/10.1101/2022.01.07.475440
https://doi.org/10.1101/2022.01.07.475440
Autor:
Michael C. Baxa, Tobin R. Sosnick
Publikováno v:
Protein Folding ISBN: 9781071617151
The formation of the transition state ensemble (TSE) represents the rate-limiting step in protein folding. The TSE is the least populated state on the pathway, and its characterization remains a challenge. Properties of the TSE can be inferred from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15840c2b02c7390f9c562948f789019c
https://doi.org/10.1007/978-1-0716-1716-8_2
https://doi.org/10.1007/978-1-0716-1716-8_2
Autor:
Michael C, Baxa, Tobin R, Sosnick
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2376
The formation of the transition state ensemble (TSE) represents the rate-limiting step in protein folding. The TSE is the least populated state on the pathway, and its characterization remains a challenge. Properties of the TSE can be inferred from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0b80f205db1300224d56eaa24289b3bb
https://pubmed.ncbi.nlm.nih.gov/34845602
https://pubmed.ncbi.nlm.nih.gov/34845602
Autor:
Paul C. Roberts, Emilio P. Mottillo, Andrea C. Baxa, Henry H.Q. Heng, Nicole Doyon-Reale, Lucie Gregoire, Wayne D. Lancaster, Raja Rabah, Eva M. Schmelz
Publikováno v:
Neoplasia: An International Journal for Oncology Research, Vol 7, Iss 10, Pp 944-956 (2005)
Studies performed to identify early events of ovarian cancer and to establish molecular markers to support early detection and development of chemopreventive regimens have been hindered by a lack of adequate cell models. Taking advantage of the spont
Externí odkaz:
https://doaj.org/article/30799dd2186c4741a5d913ab6265662a
Autor:
Srinivas Chakravarthy, Isabelle Gagnon, Michael C. Baxa, Tobin R. Sosnick, Joshua A. Riback, Joseph R. Sachleben, Xiaoxuan Lin, Patricia L. Clark
Publikováno v:
Biophysical Journal. 120:277a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a9ccf70b69007c35b4727973e303e065
https://doi.org/10.1016/j.bpj.2020.11.1762
https://doi.org/10.1016/j.bpj.2020.11.1762
Autor:
Karl F. Freed, Nabil F. Faruk, Scott Houliston, Cheryl H. Arrowsmith, Michael C. Baxa, Gabriel J. Rocklin, Xiangda Peng, Tobin R. Sosnick
Publikováno v:
Biophysical Journal. 120:116a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff9f58788760a7c0a295e35af001c584
https://doi.org/10.1016/j.bpj.2020.11.917
https://doi.org/10.1016/j.bpj.2020.11.917
Publikováno v:
Proceedings of the National Academy of Sciences. 113:4747-4752
The relationship between folding cooperativity and downhill, or barrier-free, folding of proteins under highly stabilizing conditions remains an unresolved topic, especially for proteins such as λ-repressor that fold on the microsecond timescale. Un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::509636e7ffa7603095b783ee5df42051
https://doi.org/10.1073/pnas.1522500113
https://doi.org/10.1073/pnas.1522500113
Autor:
Joshua A. Riback, Zachary P. Gates, Michael C. Baxa, Benoît Roux, Wookyung Yu, Tobin R. Sosnick, Hui Li, Stephen B. H. Kent
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(9)
The burial of hydrophobic side chains in a protein core generally is thought to be the major ingredient for stable, cooperative folding. Here, we show that, for the snow flea antifreeze protein (sfAFP), stability and cooperativity can occur without a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::684f798bf9f91b30fe0c7eb02ad2fdd7
https://pubmed.ncbi.nlm.nih.gov/28193869
https://pubmed.ncbi.nlm.nih.gov/28193869
Autor:
John J. Skinner, Michael C. Baxa, Wookyung Yu, Tobin R. Sosnick, Karl F. Freed, Elizabeth K. Gichana, James R. Hinshaw
Publikováno v:
Proceedings of the National Academy of Sciences. 111:15975-15980
Long-time molecular dynamics (MD) simulations are now able to fold small proteins reversibly to their native structures [Lindorff-Larsen K, Piana S, Dror RO, Shaw DE (2011) Science 334(6055):517-520]. These results indicate that modern force fields c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61dc71db880cc694b3c7f1ad867b0df7
https://doi.org/10.1073/pnas.1404213111
https://doi.org/10.1073/pnas.1404213111