Karen Reece |
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PhD, Physiology, University of...
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Promega
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Nucleic Acid Technologies
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Education
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Jul 2000–
Nov 2007University of Wisconsin
Physiology · PhDUSA · Madison, WI -
Jul 2000–
Aug 2002University of Wisconsin - Madison
Physiology · MSUSA · Madison -
Sep 1996–
May 2000University of Wisconsin - Madison
Biochemistry · BSUSA · Madison
Other
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LanguagesEnglish, a little Spanish
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Scientific MembershipsAlpha Chi Sigma
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Journal RefereesAnalytical Biochemistry, Biochemistry
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Other Interestsmusic, social justice
Questions and Answers (27) View all
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Answer added in DNA Extraction3 Quality DNA from swabs samplesBy Jim Mcmichael · Bucknell UniversityKaren Reece · PromegaIt looks like your problem is less with protein contamination and more with some kind of carryover (e.g. guanidine) from your purification causing hig... [more]It looks like your problem is less with protein contamination and more with some kind of carryover (e.g. guanidine) from your purification causing high A230 values.Following
Publications (2) View all
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Article: Intramolecular interactions in the N-domain of cardiac troponin C are important determinants of calcium sensitivity of force development.
Karen L Reece, Richard L Moss[show abstract] [hide abstract]
ABSTRACT: Myocardial contraction is initiated when Ca2+ binds to site II of cardiac troponin C. This 12-residue EF-hand loop (NH2-DEDGSGTVDFDE-COOH) contains six residues (bold) that coordinate Ca2+ binding and six residues that do not appear to influence Ca2+ binding directly. We have introduced six single-cysteine substitutions (italics) within site II of cTnC to investigate whether these residues are essential for Ca2+ binding affinity in isolation and Ca2+ sensitivity of force development in single muscle fibers. Ca2+ binding properties of mutant proteins were examined in solution and after substitution into rat skinned soleus fibers. Except for the serine mutation, cysteine substitution had no effect on Ca2+ binding on cTnC in solution. However, as part of the myofilament, the threonine mutation reduced Ca2+ sensitivity while the phenylalanine mutation increased Ca2+ sensitivity. Analysis of the available crystal and NMR structures reveals specific structural mechanisms for these effects.Biochemistry 06/2008; 47(18):5139-46. · 3.42 Impact Factor -
Article: Removal of contaminating calcium from buffer solutions used in calcium binding assays.
Karen L Reece, Richard L MossAnalytical Biochemistry 07/2007; 365(2):274-6. · 3.00 Impact Factor