There is a growing movement to involve undergraduate students in authentic research experiences. A variety of studies have indicated the strength of this approach in developing scientific aptitude, confidence, critical thinking skills, and increasing the likelihood to become career scientists. Course-based undergraduate research experiences (CUREs) foster opportunities for students to carry out authentic research at both primarily undergraduate and large research institutions. Here, we describe a novel CURE-based biochemistry laboratory course to explore the consequences of mutagenesis of non-conserved amino acid sites in the structure and function of the lactate dehydrogenase enzyme and demonstrate how collaborations between institutions can facilitate real research experiences at any type of institution. © 2018 by The International Union of Biochemistry and Molecular Biology, 46(3):285-296, 2018.

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Abbreviations: HPLC, high performance liquid chromatography; MS, mass spectrum; PCR, polymerase chain reaction; PLR, pinoresinol lariciresinol reductase; SDG, secoisolariciresinol diglucoside; Ubi, ubiquitin. were found to be 2.2-times higher in one of the three positive transgenic sub-lines at TB 2 B than that in the wild-type (117.9 ± 4.5 vs. 52.9 ± 19.8 µg/g, p < 0.005). To the best of our knowledge, this is the first study that elevated lignan levels in a transgenic wheat line has been successfully achieved through genetic engineering of over-expressed PLR gene. Although future studies are needed for a stably expression and more efficient transformants, the new wheat line with significantly higher SDG contents obtained from this study may have potential application in providing additive health benefits for cancer prevention.

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Immunoglobulin (Ig) domains are the most prevalent protein domain structure and share a highly conserved folding pattern; however, this structural family of proteins is also the most diverse in terms of biological roles and tissue expression. Ig domains vary significantly in amino acid sequence but share a highly conserved tryptophan in the hydrophobic core of this beta-stranded protein. Palladin is an actin binding and bundling protein that has five Ig domains and plays an important role in normal cell adhesion and motility. Mutation of the core tryptophan in one Ig domain of palladin has been identified in a pancreatic cancer cell line, suggesting a crucial role for this sole tryptophan in palladin Ig domain structure, stability, and function. We found that actin binding and bundling was not completely abolished with removal of this tryptophan despite a partially unfolded structure and significantly reduced stability of the mutant Ig domain as shown by circular dichroism investigations. In addition, this mutant palladin domain displays a tryptophan-like fluorescence attributed to an anomalous tyrosine emission at 341 nm. Our results indicate that this emission originates from a tyrosinate that may be formed in the excited ground state by proton transfer to a nearby aspartic acid residue. Furthermore, this study emphasizes the importance of tryptophan in protein structural stability and illustrates how tyrosinate emission contributions may be overlooked during the interpretation of the fluorescence properties of proteins.

Adequate dietary fiber intakes, particularly fiber from cereal grains, have been associated with a low risk of colorectal cancer (1). Wheat bran appears to protect against tumor development more consistently than other sources of plant fiber in a number of experimental colon cancer studies (2-4). Several hypotheses have been established to explain the link between wheat bran and cancer prevention, including the increase of overall GI transit time, dilution of carcinogenic compounds, release of short-chain fatty acids, and promotion of tumor suppressor signaling, among others (5-8). However, the experimental evidence by using different fiber sources or different doses on colon cancer prevention is controversial (9,10). Especially, a study conducted in the Takemoto laboratory showed that antitumor activities of wheat bran from various wheat cultivars were significantly different even when fiber content was equal (11).Lignans are a group of the phytochemicals that are composed of phenylpropane dimer linked with a 1,4-diarylbutane structure by b-b bonds. Figure 16.1 shows the chemical structure of a few prominent lignans. Lignans not only present abundantly in flaxseed but also present in various grains such as wheat (12). In wheat, lignans are located in the pericarp and aleurone layers with the highest concentration in wheat bran (13). The main lignan in wheat bran is SDG. Table 16.1 lists the contents of SDG in flaxseed, wheat bran, and some other selected plant foods.As one group of secondary metabolites, lignans are synthesized via phenylpropanoid pathway. However, the completed biosynthetic pathways to the lignans in wheat are not clear. The Lewis laboratory from the Washington State University Wheat Antioxidants, Edited by Liangli Yu

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