As we close out 2013 and navigate the foodie pleasures that tradition dictates, let’s not lose sight of the calendar ‘do over’ that a New Year brings. We get to reset our awareness, attention, appreciation, anticipation and most importantly, our actions. This is particularly effective when it’s in service to our food. — we can do this one bite at a time because that’s how it usually happens.
Here are some of the top 10 food trends we’ll be hearing about as the New Year envelops our actions and our ability to play and master the “Is It Healthy?” Game. Get set for your best healthy eating New Year ever.
Long live those kale recipes, exotic grains and vegetables. Food, real food will be taking a larger role, in awareness and in tasty experiments. Deeper connections to the farm will be a big part of our expanding awareness. Our food and our environment will become more obvious to lots more of us.
Protein has a big future as food manufacturers go macro in their marketing benefit strategies. It’s a lot simpler to tout protein , carbohydrates and fats than it is to explain why all the fillers, additives and preservatives are also part of the package. Consumers will get better educated and much savvier in the process. The food products in the marketplace will have to compete on food value instead of marketing hype and that’s good for all consumers.
Chef’s picks for the top ten food trends for 2014 according to the National Restaurant Association’s Top 20 include gluten free items gaining ground.
Gluten Free Pasta
The Food Channel says bread will rise to the top of awareness along with cell phone obsessed appetizer pairings.
Supermarket News reports that healthy and flavorful, tastes from Turkey, Israel and other areas of the Middle East will join pizza, garlic and chickpeas in popularity.
Watch for chefs riding a trend toward dairy-free to go nuts with nut milks and sauces.
Restaurants in retail sores make a comeback. Thirty years ago, retails stores kicked out their restaurants. They were too messy and not profitable enough. Big mistake. Now retailers are rediscovering the added profits from ‘dwell time’ spent by keeping hungry customers in the store. We’ve seen it in book stores with coffee shops, but retail and food always make sense. If you fed hungry customers, they’d stick around and buy more besides the food they ate.
Watch for more locally sourced food in restaurants. Super Market Guru predicts the The Emergence of the “IndieWoman”. Almost 31 million strong, the “IndieWoman” is 27 and older, lives alone and has no children and spends $50 billion on food and beverages each year. They have no time, so look for more brands to offer more semi-homemade meals that use fresh, high-quality ingredients.
Take a closer look at 2014’s trends on Pinterest to get your appetite going. The top eight healthy trends of 2014 include brussel sprouts and leafy greens in everything.
The conference and meeting industry makes a nod to healthy food along with Asian inspired and experienced based trends that are fun, entertaining or even one item pleasures.
The key trend is consumers making deeper connections to their food in 2014. Tasty, fun and healing are not incompatible and the New Year will bring new opportunities for all of us to master the “Is It Healthy?” Game one bite at a time.
Thanks to the insane geniuses at Vsauce for explaining DNA and how it works in all of us. You might want to watch this a couple of times if your human biology isn’t quite up to what it should be. It will be better than relying on more hot pockets for your nutrition and cell reproduction.
Researchers at the RIKEN Systems and Structural Biology Center and the University of Tokyo have clarified the structural basis for the biosynthesis of selenocysteine (Sec), an amino acid whose encoding mechanism offers clues about the origins of the genetic alphabet. The findings deepen our understanding of protein synthesis and lay the groundwork for advances in protein design.
One of the most remarkable aspects of translation, the process whereby genetic information is converted into proteins in cells, is its universality: nucleotide triplets (“codons”) encode a set of twenty amino acids that form the building blocks for all living organisms. Selenocysteine, the “21st amino acid” whose antioxidant properties help prevent cellular damage, is a rare exception to this rule. Structurally similar to the amino acid serine (Ser) but with an oxygen atom replaced by the micronutrient selenium (Se), selenocysteine is synthesized through a complex juggling of the cell’s translational machinery whose mechanisms remain poorly understood.
Central to this multi-step process is a Sec-specific transfer RNA (tRNASec) with an unusual structure that enables it to hijack the “stop codon” UGA to allow incorporation of selenocysteine during protein synthesis. In earlier work, the researchers identified features of tRNASec that differentiate it from other tRNA, notably the peculiar structure of a domain called the D-arm, which appeared to act as an identification marker for recognition by the selenocysteine synthesis machinery. This time, the team analyzed the D-arm’s role in the interaction of tRNASec with O-phosphoseryl-tRNA kinase (PSTK), a protein whose selective phosphorylation is essential for selenocysteine encoding.
Using X-ray crystallography, the team showed for the first time that it is the unique structure of the tRNASec D-arm which enables PSTK to distinguish tRNASec from other tRNA. Reported in the August 13th issue of Molecular Cell (online August 12th), the discovery clarifies a pivotal step in selenocysteine biosynthesis, shedding new light on the mysterious 21st amino acid and the elaborate process by which it is created.
Figure 3: Structure of the tRNASec・PSTK complex. (a) Two PSTK molecules (colored blue and green) interact with each other to form a homodimer. Each PSTK molecule binds a tRNASec molecule. PSTK consists of two independent, linker-connected domains, the N-terminal catalytic domain (NTD) and the C-terminal domain (CTD). These domains independently bind tRNASec. (b) A close-up view of one of the PSTK molecules bound to tRNASec. The N-terminal domain (NTD) and the C-terminal domain (CTD) of PSTK interact with the acceptor arm (colored pink) and the D arm (light blue), respectively. PSTK does not interact with the tRNASec anticodon complementary to the UGA codon.
Figure 1: Comparison of selenocysteine (Sec) to the structurally similar amino aids serine (Ser) and cysteine (Cys).
Figure 2: Selenocysteine biosynthesis. (Top) tRNASec is first ligated with serine to form Ser-tRNASec. The seryl moiety of Ser-tRNASec is then phosphorylated by PSTK to yield P-Ser-tRNASec, which is converted to Sec-tRNASec and used on the ribosome to insert Sec into a specific site in a nascent polypeptide of selenoproteins. (Bottom) In the case of the standard amino acid serine, tRNASer is ligated with serine and directly used for translation. Ser-tRNASer is not a substrate of PSTK.
Figure 4: Interaction between the unique D arm of tRNASec and the PSTK CTD. (Top) Comparison of the secondary structure of tRNASec to that of a canonical tRNA. The tRNASec D arm consists of a six base-pair stem (D stem) and a four-nucleotide loop (D loop), in contrast with the 3–4 base-pair D stem and the 7–11 nucleotide D loop of the canonical tRNA. (Bottom) The D arm of tRNASec (colored light blue) snugly interacts with the PSTK CTD (green), whereas the D arm of the standard tRNA (blue) does not fit the PSTK CTD.
Figure 5: tRNASec recognition by PSTK. The enzymatic activity of PSTK is governed by the specific interaction between its CTD and the unique D arm of tRNASec. The tight binding of the CTD to the D arm ensures that the N-terminal catalytic domain binds to the end of the acceptor arm, where the phosphorylation reaction occurs. In contrast, the CTD does not fit the D arm of canonical tRNAs, and thus PSTK does not act on them, segregating the Sec insertion pathway from the normal amino-acid translation process.