The T3 Method (“T3 It!”): Transcribe → Translate → Transform

Author:

Malas Brett1

Affiliation:

1. BRETT MALAS is a National Board-Certified Teacher, author, lecturer, and associate with the Center for Teacher Effectiveness, and high school science teacher with degrees in biology and paleontology; e-mail: t3method@gmail.com

Abstract

Traditional transcription-translation exercises are instructionally incomplete by failing to link prescriptive genetic information with protein structure and function. The T3 Method solves this problem by adding a conceptually powerful yet easily learned third step where students use simple protein folding codes to transform their translations into corresponding protein structural models. This brings structural sense to sequence and makes the information-to-proteins connection that is so profoundly important to understand in biology more directly evident, experiential, and intrinsically meaningful. The T3 Method has further utility, proving versatile and adaptive to a wide range of academic levels and learning contexts, with possibilities for differentiated instruction, application, and extension.

Publisher

University of California Press

Subject

General Agricultural and Biological Sciences,Agricultural and Biological Sciences (miscellaneous),Education

Reference25 articles.

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3. Bradley, L. H., Thumfort, P. P., & Hecht, M. H. (2006). De novo proteins from binary-patterned combinatorial libraries. In R. Guerois & M. López de la Paz (Eds.), Protein Design (pp. 53–69). Totowa, NJ: Humana Press.

4. Bradley, L. H., Wei, Y., Thumfort, P., Wurth, C., & Hecht, M. H. (2007). Protein design by binary patterning of polar and nonpolar amino acids. In K. M. Arndt & K. M. Müller (Eds.), Protein engineering protocols (pp. 155–166). Totowa, NJ: Humana Press.

5. Broome, B., & Hecht, M. (2000). Nature Disfavors Sequences of Alternating Polar and Non-polar Amino Acids: Implications for Amyloidogenesis. Journal of Molecular Biology, 296, 961–968.

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