Amazing gift for yoga students

Not sure how I came across this yoga channel, but WOW! I love it. There’s something about this woman that shines through that will make her a superstar if she doesn’t lose track of that innocence and willingness to share. I’m talking about Dashama and her yoga/lifestyle videos that she posts on YouTube.

Here is one of her postings showing how to perform a handstand.

I am so motivated to perform this handstand right now! The level of detail she goes into when instructing is great. After seeing this video the first time, I started following her advice of ‘locking down the lats’ when performing the Vasisthasasa (Side Plank Pose) and I actually found that I could perform this – difficult – move for more than just a couple seconds. When I don’t ‘lock down the lats’, I end up with a sore shoulder in no time at all.

Here’s another one she put up a couple years ago.

She absolutely makes this look easy! I also love the fact that she’s introduced me to moves that are, well, not all that standard for the typical yoga class. A double warrior, I’m looking forward to my next workout.
She’s so animated and clearly unconcerned. It’s like she just puts it all out there with confidence knowing that she is what she is.

Here’s another that I’m going to add to my practice.

Dang. What a hold on the standing splits. That is truly inspiring. I wonder if I’ll ever be able to do that forward bend like she does.

I’m hoping that one of these days I’ll get to practice with her. Maybe if I stick with it long enough, our paths will cross and I’ll be able to show her that she taught me how to do a handstand!


What is a (type 2) diabetic to do?

As it turns out, there are more than just a few people that I know that have type 2 diabetes or they have a family history of it. When I hear them talk about it, it’s quite often that there is a tone of eventuality as if it will be on their doorstep before too long. In a way it’s sad to hear that people accept that as their fate without really looking any further.

If you’re lucky (like me), you’ll ask if there is a ‘cure’ or ask to see how other people ‘cure’ themselves of these symptoms. And, if you’re persistent (like me), you’ll Google up your favorite phrase like “Raw Food Diabetes cures”. When I perform that query, I get 218k hits.

The second non-sponsored link returned is a link to Amazon and a book by Gabriel Cousens:

The third link is to a little article at TheBestOfRawFood that’s linked in the trailer for Simply Raw – Reversing Diabetes in 30 days. It’s pretty inspiring, so I figured I’d also include it here. I highly recommend giving it the five minutes.

Now, things even get better. Not only can you pick up the DVD for a nominal 30 bucks (and if you really think about that, that’s less than what you’d spend going out for one dinner and drinks), but you can actually attend a seminar where they help you reverse the diabetic process. (note, I am not getting paid to push this DVD or the program! I’m writing this out of the goodness of my heart.)

You’ll want to visit the Tree of Life Rejuvenation Center, which is their main page. Or visit the There is a Cure for Diabetes! page.

As it turns out, I took the time to enquire for a brochure. It’s the 2009 brochure. If you don’t have the will power to change your life after watching the DVD, you can sign up and take the program for about 13k.

Let’s see. The last vacation I took to Hawaii cost me about $700 a day. If I’d stayed for 21 days, that trip would have cost almost 15k. Seems to me that attending the program would be better than a good vacation, it would be life altering!

Here is the page where you can request your own brochure!

Everyone gets to make their own choices in life. The fact that you’re reading this may mean that you were looking for a little encouragement or that you’re simply looking outside the standard dogma preached to people today – there is no cure for diabetes. Yet, if you no longer have the symptoms, do you still have the disease?

That’s the real challenge.

Have a good day!

A link to the 50 Best Raw Food Blogs

It’s quite often that when I come up with an idea for a blog article someone else has already put together something similar. In this case, RadiologyTechniciansSchools has done just that regarding the 50 Best Blogs for Raw Food Recipes & Inspiration. What a great collection of links!

If you want to learn about the raw food community, this is one of the best collections of links that I’ve found.


You full of crap?

I’m willing to bet that everyone is. Lol. 

When surfing yesterday, I came across an older Raw Life Health Show video on YouTube that caught my eye. It had both Cacao and Colon in the title, so I couldn’t help but wonder if chocolate was …  ah… Let’s not go there!

I do have to admit that I’ve had a couple colonics before. I’ve suffered from allergies for as long as I can remember, but when I finished my first colonic I experienced three days of pure clean breathing! I couldn’t believe it. It was during allergy season and my nose just didn’t act up. I don’t think I’ll ever forget that experience.

Now that video also had the word cacao. If you’ve read through the archives at all you’ll know that I love my raw chocolate. Well, there is cacao in that and it’s not a small amount.

So, anyway, I clicked and watched the video. I figured I’d see what these guys had to say.

Part way through the video I distinctly remember getting the impression that the Dr. being interviewed wasn’t telling the whole truth. Might be that there is a conflict of interest or something, but the basic information is worth the time. Hopefully you will not get the same feeling.

Before giving you the links, I’ll have to state that I am a firm believer that the body cures itself. If given the proper tools (molecules and energy) the body will always strive for perfect health. The only thing that we should be striving for is pure thoughts – let the body do what it does. Meanwhile, we get to use the body to live out our dreams and manifest our thoughts.

If nothing else, if you cut yourself, it’s the body that heals the wound – not the bandaid that you place over the cut. You didn’t have to think about the healing process or help it along other then to pay attention to any sensation of pain.

Back to the videos. Turns out that this interview can be found on the YouTube channel “The Raw Life Health Show with Paul Nison” – thedurianking’s channel (Google that up if the link above doesn’t work).  It is a four part series where Paul interviews Dr. Charles Partito of

Try to keep an open mind for the doctor can sound like a salesman during different parts of the interview, but he does have interesting information to share.

First segment: How important is it to cleanse the colon?

Second segment: Are all probiotics the same? (#227)

Third segment: Are herbs really healthy? (#228)

Fourth segment: Is Cacao Healthy and Colon cleansing #230

After having watched this, I looked up the websites. The Ejuva website has a highly motivating video about cleaning the colon on the “program” page (see the link). Try to overlook some of the pictures. The testimonial page seems a bit contrived, but Google (I’m sure) can help me find some real customers. If I find some, I’ll link them in here.

Lastly, if I can find some real testimonials, I might just give this cleansing program a try. And, the next time I go to refill my probiotics, I think I’ll order up Moflora. Seems like a reasonable price.

Heat changes molecules

Why is this interesting and why should we care?

You ever try to grow a seed after heating it? Everyone knows that if you heat something too much you kill it. We all take that for granted. We learn that at a young age and simply don’t question it. Well, that is what we will do now.

Why did heat kill the seed?

And, probably more important:

Did the heat kill the seed?

Both questions are kind of puzzling. Why would anyone question how the seed died?

To understand this a bit better, let’s look at the first signs that a seed provides to indicate that it is alive. That process has a well known name, germination. Here is what the Wikipedia has to say about germination:

Germination is the process in which a plant or fungus emerges from a seed or spore and begins growth. The most common example of germination is the sprouting of a seedling from a seed of an angiosperm or gymnosperm.

Germination is the growth of an embryonic plant contained within a seed; it results in the formation of the seedling.

So, if the seedling can germinate, we know that the seed is alive. I know this next part is going to sound really simple, but what makes a seed germinate? Yes, I know. This is another one of those things that just about everyone also takes for granted. At the same Wikipedia link, we see:

Seed germination depends on both internal and external conditions. The most important internal factors include temperature, water, oxygen and sometimes light or darkness.

As it turns out, the requirements needed for that little seedling align pretty well with what we humans need to stay alive. But let’s continue to focus on the seedling.

If you look closely at what the Wikipedia says about the effect that water has on germination, we find some interesting points:

Water – is required for germination. Mature seeds are often extremely dry and need to take in significant amounts of water, relative to the dry weight of the seed, before cellular metabolism and growth can resume. Most seeds need enough water to moisten the seeds but not enough to soak them. The uptake of water by seeds is called imbibition, which leads to the swelling and the breaking of the seed coat. When seeds are formed, most plants store a food reserve with the seed, such as starch, proteins, or oils. This food reserve provides nourishment to the growing embryo. When the seed imbibes water, hydrolytic enzymes are activated which break down these stored food resources into metabolically useful chemicals.[2]

So, if the seed is alive, when it takes in water and oxygen at the right temperature and with the correct amount of light, enzymes are activated which break down the stored resources into usable building blocks that the plant can use to grow.

What I find interesting is that the Wikipedia can always take a simple subject and confuse it with a lot of big words. What are hydrolytic enzymes? And what are metabolically useful chemicals?

From this link, we find a hint regarding what a hydrolytic enzyme is:

In biochemistry, a hydrolase is an enzyme that catalyzes the hydrolysis of a chemical bond.

Looking closer, Hydrolysis is:

Hydrolysis is a chemical reaction during which molecules of water (H2O) are split into hydrogen cations (H+) (conventionally referred to as protons) and hydroxide anions (OH) in the process of a chemical mechanism.[1][2] It is the type of reaction that is used to break down certain polymers, especially those made by step-growth polymerization. Such polymer degradation is usually catalysed by either acid, e.g., concentrated sulfuric acid (H2SO4), or alkali, e.g., sodium hydroxide (NaOH) attack, often increasing with their strength or pH.

Hydrolysis is distinct from hydration. In hydration, the hydrated molecule does not “lyse” (break into two new compounds).

Something worth noting here is that when something goes through hydrolysis, it is a chemical reaction that splits down certain polymers. Also, form the seed perspective, it’s using enzymes to perform this function. (What we don’t cover here is the reference to pH. That is a article for another day!) Yet, what is a polymer?

A polymer is a large molecule (macromolecule) composed of repeating structural units typically connected by covalent chemical bonds. While polymer in popular usage suggests plastic, the term actually refers to a large class of natural and synthetic materials with a wide variety of properties.

Because of the extraordinary range of properties accessible in polymeric materials,[2] they play an essential and ubiquitous role in everyday life[3]—from plastics and elastomers on the one hand to natural biopolymers such as DNA and proteins that are essential for life on the other.

So the addition of water to the seed enables it to put its water sensitive enzymes to work breaking down the stored protein or other long molecules that have covalent chemical bonds. The seed can convert long macromolecules and proteins into what it needs to grow by simply applying water based enzymes.

As a reminder:

 A chemical bond is an attraction between atoms or molecules and allows the formation of chemical compounds, which contain two or more atoms. A chemical bond is the attraction caused by the electromagnetic force between opposing charges, either between electrons and nuclei, or as the result of a dipole attraction. The strength of bonds varies considerably; there are “strong bonds” such as covalent or ionic bonds and “weak bonds” such as dipole-dipole interactions, the London dispersion force and hydrogen bonding.

If you remember from a previous article (Is food another form of light) you’d remember that when the chemical bonds break down, the molecules give off electromagnetic energy (light) in the process. Thus, light is part of the growing process – from the inside out!

So, if I’m following this correctly, the enzymes are the molecules that first go to work in the germination process that will eventually show up to us humans as a growing plant.

Makes sense that we look at enzymes:

Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions.[1][2] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, called the products. Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.

Like all catalysts, enzymes work by lowering the activation energy (Ea) for a reaction, thus dramatically increasing the rate of the reaction. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more specific. Enzymes are known to catalyze about 4,000 biochemical reactions.[3] A few RNA molecules called ribozymes also catalyze reactions, with an important example being some parts of the ribosome.[4][5] Synthetic molecules called artificial enzymes also display enzyme-like catalysis.[6]

Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, chemical environment (e.g., pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew).

Looking a little deeper into the enzyme link at Wikipedia:

Like all proteins, enzymes are made as long, linear chains of amino acids that fold to produce a three-dimensional product. Each unique amino acid sequence produces a specific structure, which has unique properties. Individual protein chains may sometimes group together to form a protein complex. Most enzymes can be denatured—that is, unfolded and inactivated—by heating or chemical denaturants, which disrupt the three-dimensional structure of the protein. Depending on the enzyme, denaturation may be reversible or irreversible.

There they go using another collection of relatively unknown words.  Let’s look at denatured:

Denaturation is a process in which proteins or nucleic acids lose their tertiary structure and secondary structure by application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death.

When food is cooked, some of its proteins become denatured.

Hey, that is the link I was looking for! We should eventually come back to that.

First, let’s look back at our question: did the heat kill the seed? Logically, it would seem that the heat denatured the proteins that make up the enzymes that are used to break down the stored resources that the seed needs to grow.

Looking at this a different way, after applying heat, the seed has no means of convert the stored resources (proteins and carbohydrates) into useful building blocks for growth. Because of this, the seed is effectively locked in a state of not being able to use its energy reserves.

Ultimately, the heat killed the seed. But why the heat killed the seed has to make you wonder. If heat can denature the proteins that are needed by the seed to life and grow, what kind of ramifications does it have on the human body? Doesn’t the human body need enzymes – just like the seedling does? More importantly, if heat can denature enzymes, which are protein molecules, it would hold that heat would change all types of protein molecules.

We see what heat does to proteins, what about carbohydrates?

Let’s look that up:

A carbohydrate is an organic compound with the general formula Cm(H2O)n, that is, consists only of carbon, hydrogen and oxygen, the last two in the 2:1 atom ratio. Carbohydrates can be viewed as hydrates of carbon, hence their name.

Monosaccharides can be linked together into what are called polysaccharides (or oligosaccharides) in a large variety of ways. Many carbohydrates contain one or more modified monosaccharide units that have had one or more groups replaced or removed. For example, deoxyribose, a component of DNA, is a modified version of ribose; chitin is composed of repeating units of N-acetylglucosamine, a nitrogen-containing form of glucose.

And from the polysaccharides link we find:

Polysaccharides have a general formula of Cx(H2O)y where x is usually a large number between 200 and 2500. Considering that the repeating units in the polymer backbone are often six-carbon monosaccharides, the general formula can also be represented as (C6H10O5)n where 40≤n≤3000.

This polysacchraride is not simple sugar!

Yet these longer molecular structures don’t taste all that great, nor do the digest readily until they are broken down into smaller pieces. Some enzymes can perform this work, but the fastest process is heating. The heating process breaks the chemical bonds that attach the longer molecules into smaller ones.

This can be seen in the simple process of cooking a potato. Does it taste better raw, or cooked? Anyone can tell you that it tastes sweater after cooking. That’s because the longer starch molecules have been broken down into simpler sugars with register as sweet to the taste budds.

What’s also interesting is that plants have developed molecules that humans have a hard time with. Specifically, if we look up Cellulose, we find:

Cellulose is an organic compound with the formula (C6H10O5)n, a polysaccharide consisting of a linear chain of several hundred to over ten thousand β(1→4) linked D-glucose units.[2][3]

Cellulose is the structural component of the primary cell wall of green plants, many forms of algae and the oomycetes. Some species of bacteria secrete it to form biofilms. Cellulose is the most common organic compound on Earth. About 33 percent of all plant matter is cellulose (the cellulose content of cotton is 90 percent and that of wood is 40-50 percent).

It’s a really long polysaccharide that forms the cell wall in plants. It’s something that we don’t digest well. Cows and horses do a much better job handling this molecule with the help of microbes. Yet, the human solution to getting around this problem is to cook it.  Applying heat breaks apart the cell wall which makes what’s inside the cell available to the body. Yet heating also denatures other elements of the cell.

So, what do we do?

It would seem that heating destroys key elements of our food. Elements like enzymes that we need to break down other molecules. At the same time, our bodies can’t get to all the ‘food’ in what we eat unless we can get past the larger polysaccharides that block our digestive way.

If we want the best of both worlds here, we’re going to have to get to what’s in the cell without ingesting the larger indigestible molecules. Off hand, I can think of two techniques:

  • Juicing

Here we simply squeeze what’s inside the cells out. If done with little friction, which causes heat, the results should be pure and highly digestible by the body.

  • Blending

Similar to juicing, a good blender will apply enough force to the cells to get them to break apart rendering a mixture that still contains the fibrous material along with the ‘nectar’ found inside the cells.

Both of these techniques seem like great alternatives then heating.

This investigation still leaves a number of unanswered questions.

If heating denatures proteins (destroys them) and you consume them. Can your body still use them effectively? Do these fractured pieces of molecules find function in the body? Or, do they create a situation like looking for an intact glass in a pile of glass fragments? (A nearly impossible task for surviving enzymes.) Also, might the body actually use the denatured proteins thinking that they were the real intact versions? What might this cause?

The more I learn about how heat changes molecules, the more I ask myself is it really worth consuming denatured food? Are there other alternatives like juicing and blending – or simply eating the food unaltered? What might be the best choice?

I guess I’m going to have to investigate whether or not the body can create its own enzymes and how that is done. On top of that, I’ll have to look into mucus and see what that’s made of. I heard it was undigested proteins – the above information could support that idea. Pausing and reflecting on the above, I can understand why so many people have runny noses!

The real question is what are you going to do? It seems pretty clear to me that we should be consuming foods with unaltered molecular structures. I’m going to make it a point to do so.  What about you?