R
Randy M. Whittal
Researcher at University of Alberta
Publications - 81
Citations - 5149
Randy M. Whittal is an academic researcher from University of Alberta. The author has contributed to research in topics: Mass spectrometry & Steroidogenic acute regulatory protein. The author has an hindex of 34, co-authored 77 publications receiving 4719 citations. Previous affiliations of Randy M. Whittal include University of California, San Francisco & Mercer University.
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Interferences and contaminants encountered in modern mass spectrometry
TL;DR: This review/tutorial summarizes current literature on reported contaminants and introduces a number of novel interferences that have been observed and identified in laboratories over the past decade, including both compounds of proteinaceous and non-proteinaceous nature.
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Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile
Mary C. Rea,Clarissa S. Sit,Evelyn M. Clayton,Paula M. O'Connor,Randy M. Whittal,Jing Zheng,John C. Vederas,R. Paul Ross,Colin Hill +8 more
TL;DR: Thuricin CD is a two-component antimicrobial peptide system with sulfur to α-carbon linkages that may have potential as a targeted therapy in the treatment of CDAD while also reducing collateral impact on the commensal flora.
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Naphthenic acids and other acid-extractables in water samples from Alberta: what is being measured?
TL;DR: It appears that the term "naphthenic acids", which has been used to describe the toxic extractable compounds in OSPW, should be replaced by a term such as "oil sands tailings water acid-extractable organics (OSTWAEO)".
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Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry.
Randy M. Whittal,Haydn L. Ball,Fred E. Cohen,Alma L. Burlingame,Stanley B. Prusiner,Michael A. Baldwin +5 more
TL;DR: Although the structure of the four‐octarepeat peptide is not affected by pH changes in the absence of Cu2+, as judged by circular dichroism, Cu2+ binding induces a modest change at pH 6 and a major structural perturbation at pH 7.4.
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The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule
TL;DR: As the mitochondrial proton pump results in an electrochemical gradient, and as StAR must unfold during mitochondrial entry, StAR probably undergoes a similar conformational shift to an extended structure while interacting with the mitochondrial outer membrane, allowing this apparent molten globule form to act as an on/off switch for cholesterol entry into the mitochondria.