Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Irina A. Shkel"'
Publikováno v:
Biophysical Journal. 122:63a-64a
Autor:
Amanda C. Drennan, Irina A. Shkel, Clare Kai Cimperman, Sara Heitkamp, M. A. Sridevi, M. T. Record, Katelyn Callies, Hui Wang, Dylan Plaskon, Munish Chhabra, Christina McNerney, Raashi Sreenivasan
Publikováno v:
Biochemistry. 59:1565-1581
FRET (fluorescence resonance energy transfer) between far-upstream(-100) and downstream(+14) cyanine dyes showed extensive bending/wrapping of λPR promoter DNA on E. coli RNA polymerase (RNAP) in c...
Autor:
Alexander G. Kozlov, Xian Cheng, Hongshan Zhang, Min Kyung Shinn, Elizabeth Weiland, Binh Nguyen, Irina A. Shkel, Emily Zytkiewicz, Ilya J. Finkelstein, M. Thomas Record, Timothy M. Lohman
Publikováno v:
J Mol Biol
E. coli single-stranded-DNA binding protein (EcSSB) displays nearest-neighbor (NN) and non-nearest-neighbor (NNN)) cooperativity in binding ssDNA during genome maintenance. NNN cooperativity requires the intrinsically-disordered linkers (IDL) of the
Autor:
Kate L. Henderson, Claire Evensen, Lindsey C. Felth, Irina A. Shkel, Cristen Molzahn, Dylan Plaskon, M. Thomas Record, Sarah Dyke
Publikováno v:
Proc Natl Acad Sci U S A
Transcription initiation is highly regulated by promoter sequence, transcription factors, and ligands. All known transcription inhibitors, an important class of antibiotics, act in initiation. To understand regulation and inhibition, the biophysical
Autor:
Guanyu Liao, Irina A. Shkel, Claire Evensen, Kate L. Henderson, Lindsey C. Felth, Sarah Dyke, M. Thomas Record, Cristen Molzahn
Publikováno v:
Biochemistry
To determine the step-by-step kinetics and mechanism of transcription initiation and escape by E. coli RNA polymerase from the λPR promoter, we quantify the accumulation and decay of transient short RNA intermediates on the pathway to promoter escap
Autor:
Kate L. Henderson, Sarah Dyke, Irina A. Shkel, Claire Evensen, Cristen Molzahn, Lindsey C. Felth, M. Thomas Record, Dylan Plaskon
In transcription initiation, specific contacts between RNA polymerase (RNAP) and promoter DNA are disrupted as the RNA-DNA hybrid advances into the cleft, resulting in escape of RNAP. From the pattern of large and small rate constants for steps of in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::287649487651eb36b82def82b04ae2ca
https://doi.org/10.1101/2020.09.11.293670
https://doi.org/10.1101/2020.09.11.293670
Folding and other protein self-assembly processes are driven by favorable interactions between O, N, and C unified atoms of the polypeptide backbone and sidechains. These processes are perturbed by solutes that interact with these atoms differently t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e15989d92917dc3c4dcd077158da33f
https://doi.org/10.1101/2020.05.26.104851
https://doi.org/10.1101/2020.05.26.104851
Autor:
Raashi, Sreenivasan, Irina A, Shkel, Munish, Chhabra, Amanda, Drennan, Sara, Heitkamp, Hao-Che, Wang, Malavika A, Sridevi, Dylan, Plaskon, Christina, McNerney, Katelyn, Callies, Clare K, Cimperman, M Thomas, Record
Publikováno v:
Biochemistry
FRET (fluorescence resonance energy transfer) between far-upstream(−100) and downstream(+14) cyanine dyes showed extensive bending/wrapping of λP(R) promoter DNA on E. coli RNA polymerase (RNAP) in closed and open complexes (CC, OC). Here we deter
Autor:
Katelyn Callies, Munish Chhabra, Irina A. Shkel, M. T. Record, Christina McNerney, M. A. Sridevi, Hui Wang, Raashi Sreenivasan, Amanda C. Drennan, Dylan Plaskon, Clare Kai Cimperman, Sara Heitkamp
FRET (fluorescence energy transfer) between far-upstream (-100) and downstream (+14) cyanine dyes showed extensive bending/wrapping of λPR promoter DNA on E. coli RNA polymerase (RNAP) in closed and open complexes (CC, OC). Here we determine the kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a0b9b7c1cb1d653b07bd1954c117858
https://doi.org/10.1101/2020.02.04.932780
https://doi.org/10.1101/2020.02.04.932780
Autor:
Xian Cheng, M. Thomas Record, Irina A. Shkel, John Henrich, David Lambert, Cristen Molzahn, Kevin O'Connor
Publikováno v:
Journal of the American Chemical Society. 139:9885-9894
Quantitative information about amide interactions in water is needed to understand their contributions to protein folding and amide effects on aqueous processes and to compare with computer simulations. Here we quantify interactions of urea, alkylate