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Stanley C. Gill
Researcher at University of Oregon
Publications - 6
Citations - 5310
Stanley C. Gill is an academic researcher from University of Oregon. The author has contributed to research in topics: RNA polymerase & Transcription factor II D. The author has an hindex of 6, co-authored 6 publications receiving 5164 citations.
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Journal ArticleDOI
Calculation of protein extinction coefficients from amino acid sequence data
Stanley C. Gill,P H von Hippel +1 more
TL;DR: In this article, a method for calculating accurate molar extinction coefficients for proteins at 280 nm, simply from knowledge of the amino acid composition, was presented, and the method was calibrated against 18 "normal" globular proteins.
Journal ArticleDOI
Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex.
TL;DR: It is found that the effective binding affinity of sigma 70 for core polymerase within the "open" promoter-polymerase complex is at least 500-fold greater than that of NusA.
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Physical properties of the Escherichia coli transcription termination factor rho. 1. Association states and geometry of the rho hexamer.
TL;DR: The results show that rho exists predominantly as a hexamer under approximately physiological conditions and that this hexamer is in equilibrium with both lower and higher states of association that may also have physiological relevance.
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Escherichia coli σ70 and NusA proteins: II. Physical properties and self-association states
TL;DR: In this paper, the physical properties and potential for self-association of the Escherichia coli transcription factors, σ 70 and NusA, were examined by a combination of chemical crosslinking, equilibrium and velocity sedimentation, quasi-elastic light scattering, and small-angle X-ray scattering.
Journal ArticleDOI
Thermodynamic analysis of the transcription cycle in E. coli
TL;DR: This paper reviews recent biophysical studies of the interactions of the transcriptional regulatory proteins, sigma 70 and NusA, with themselves and with core RNA polymerase in solution, as well as with core polymerase within the transcription complex.