5 Foods to Eat to Increase Protein

There are a lot of foods that are rich in proteins, but these protein-rich foods about to be mentioned are essential in increasing the amount of protein in your body. They are all nutritious and good for you, so there is no reason why not to eat them.

Beef and Pork:
One of the best foods to eat when you need protein would have to be lean red meat like beef and pork. A portion of beef and pork would be characterized as having one ounce of each in it according to the American Diabetes Association. There are about 7 grams of protein in each portion and serving of beef and pork. Therefore, this is a great way of getting protein into your body. You can definitely have more than one portion of meat, so there is an opportunity to gain a lot of protein with each meal that beef and pork are in that you digest.

Chicken and Turkey:
Chicken and turkey are both great alternatives for beef and pork. Even though they are not red meat, the nutritious content and amount of protein in each is a lot. Chicken breast, turkey cutlets, drumsticks, cornish hens, thigh, duck, and goose each contain 7 grams of protein per ounce as well. Although 7 grams is a lot of protein, there are ways to get rid of the excess fat in each kind of meat. One can get rid of excess fat by removing all skin and visible fats.

Milk and Dairy:
Milk can be a great source of protein from a variety of animals. Some of these animals include cow and goat. The portion for these kinds of milk, rice, and soy is 8 fl. oz. Other ways of getting protein are cheese, yogurt, and cottage cheese. Every ounce of any of these three would provide a person with 7 grams of protein. Additionally, eating one whole egg or eating 2 egg whites provide a person with 7 grams of protein per egg, which is the same as most meats.

Vegetarian Foods:
It can be difficult for vegetarians to get as much protein as they should into their body because there are less options available to them, but it is still possible. There are still a myriad of options a vegetarian has in order to get protein into their body. Soy is a great protein source for vegetarians, as is tofu. Four ounces of soy gives off the same amount of protein as one ounce of chicken (seven ounces). Most packages of vegetarian foods actually have about 14 ounces of protein in them.

Nuts and Seeds:
There are a lot of snacks which can be alternatives to protein bars. These alternatives are in the form of nuts and seeds. Each ounce of nuts provides 7 grams of protein as well. Instead of having chicken, nuts can be taken to get these necessary grams of protein. Even great-tasting seeds, like sunflower seeds, have 7 grams of protein in them for one tablespoon serving. Thus, you can eat healthy and maintain high protein levels while still eating food you enjoy.

Protein Stability and Protein Folding

Protein stability is the net balance of forces which allow someone to tell whether or not the protein will be denatured. This is also referred to as thermodynamic stability. The net stability can be defined as the difference in free energy between the native and denatured state. These two values can be called Gn and Gu.

In the previous blog post, free energy was introduced as related to free energy. The Gibbs Free Energy value can be calculated using a variety of equations. In fact, there are four ways to calculate this value. The four ways include delta G = delta H - T (delta S), the difference between the free energies of products and reactants, Hess's Law, and delta G = delta Go + RTlnQ.

Decreasing the energy of the folded state or increasing the energy of the unfolded state have the same effect on delta G. The equation normally used to calculate the free energy can be taken from delta G = Gn - Gu = -RTlnK. In this case, the K would be equal to the fraction folded divided by the fraction unfolded. The reason why this practice has so much significance is because of the multitude of drugs that can be made if different proteins were seen as more stable. Various new formulas for different protein combinations can be made, which may be able to make them safer to sell in pharmacies.

We will take this formula and put it into good use through practice! We can measure the difference in free energy in the unfolded and folded states. The average stability of a monomeric small protein is about 5-10 kcal/mol. Therefore, when plugged into the equation, an aqueous solution at room temperature would have a ratio of 20000000:1 in terms of folded to unfolded. This value of K can also be looked at as the ratio of the forward and reverse rate constants. When delta G is graphed against Denaturant or Urea, the graph typically comes out to be downward sloping, signalling a drop in the amount of free energy changed.

The Van't Hoff Equation can also be written as dlnK/d(1/T) = -H/R. Thus, when Van'T Hoff plots (lnK vs. 1/T) are made, the thermal denaturation of proteins are non-linear, indicating that H varies with temperature. This implies that the heat capacity for the folded and unfolded proteins are different.

Free Energy of Protein Folding

There are a lot of benefits of understanding the free energy in protein folding. First, many proteins are used in industrialized products, including in a lot of what one puts into the body. These proteins must be stable in order to be taken in by the body. If these proteins have a slight risk of being bad for people, then these proteins cannot be sold to consumers. Another reason protein sequencing would be beneficial is because researchers believe that proteins can be denatured and still work. Instead of maintaining their shape, the proteins can still do daily life functions. One last reason why protein sequencing is helpful is because it can limit the amount of procedures that need to be done to the proteins. Some of the superfluous procedures, including X-rays crystallography and Nuclear Magnetic Resonance, will not need to be performed anymore if scientists had a better understanding of free energy.

Before we understand free energy in protein folding, we must understand free energy. Gibbs free energy, synonymous with free energy, is defined as the enthalpy of the system minus the product of the temperature times the entropy of the system. This is denoted by the equation G = H - TS. The free energy of the system is a state function because the thermodynamic functions inside of the equation, including H and S, are both state functions as well. If you want to know more, watch the video provided. It is a presentation by Paul Andersen explaining Gibbs free energy.

When proteins denature, then the primary functions of the proteins do not work. The willingness and ability for proteins to be flexible is calculated by measuring the free energy of various proteins. However, this free energy value might be more and more difficult to solve because there is a different energy landscape for each state of the protein, whether it is neutral, charged, folded, intermediate, or even unfolded. These various states allow there to be many mistakes that can occur when trying to calculate the free energy of a system. Therefore, if we understand the protein sequences better, the free energy might be easier to solve for. The state in which it is in might be able to help scientists predict what the value of the free energy is. Next post we will look into how to actually calculate this value and what state the protein must be in.

Thermodynamics and Protein Folding

There are many chemical reactions that occur in the universe. These reactions can be considered non- spontaneous or spontaneous. This all depends on the entropy that is found in the chemical equation. The chemical reactions that are categorized as being spontaneous are also known as downhill; whereas the reactions classified as being non-spontaneous are known as going uphill. So what causes chemists to label these reactions in different ways? Well, we must first need to learn more about thermodynamics and entropy. By watching the video above, you should get a better understanding of thermodynamics, and how they relate to protein folding.

Sugar Solubility and Intake

In exercise drinks such as Gatorade and Powerade, sugar is the main fuel source for the body. These drinks contain simple sugars because they are absorbed into the body faster and can be used as energy faster.  Athletes depend on these simple sugars as fuel and they need them for better performance.  For example, someone who races in a sport such as swimming or track will use these fast dissolving sugars as a quick burst of energy for a sprint.  However, they must monitor their intake of the sugars; they must take the appropriate amount and take it with the correct frequency.  When someone drinks Gatorade and the sugars enter their body, they are absorbed into the bloodstream quickly.  The pancreas must pump out insulin in order to compensate for the rise in blood sugar, also known as hyperglycemia.  But the sugars dissolve so quickly that the actual amount of them is overestimated and there is always insulin left over.  This extra insulin is stored as fat in the body, which is bad for the athlete.  In order to prevent this from happening, the athlete needs to have a continuous and constant intake of these sugars so that the blood sugar will not spike and there will not be extra insulin left over in the body.  Although it is good that these simple sugars can be used as fuel quickly, a lot of athletes make the mistake of ignoring the importance of intake frequency.  

This issue is caused because of the simple sugars' solubility properties.  Fructose is the most soluble of all the simple sugars.  In solutions, like dissolves like, meaning polar compounds will dissolve polar compounds and nonpolar compounds will dissolve nonpolar compounds.  Fructose is polar so it will easily dissolve in water, a polar solvent.  In addition, it is a smaller compound so it will dissolve faster than a larger one, such as sucrose, a disaccharide. 

Casein Proteins and Solubility

Milk proteins are some of the best proteins for their nutritional and technological value. Proteins are often a big part of peoples' diets, especially because they provide the essential amino acids and are big sources of nitrogen. Milk proteins have the best nutritional value compared to other proteins because of the high content of essential amino acids. Additionally, the good digestibility can also add to the great nutritional value.

Caseins and whey proteins are the two main protein groups that are found in milk. Caseins are found in 80 % of proteins in most milk, but are isolated from milk by acid. The acid precipitation is performed at a pH of 4.6, which is where caseins precipitate and whey proteins remain soluble. Caseins are often flexible and heat stable proteins.

The other 20 % of proteins in milk is composed of whey protein. Whey proteins are also known as proteins in milk that can remain soluble after acid precipitation, which is often found in milk. The whey protein acid that is used is formally known as acid whey, or informally as sweet whey. Whey proteins are globular proteins that are soluble over a broad pH range.

Most of the time, whey proteins have been considered as a more balanced and superior alternative to casein. The amino acids that are found in whey appear at a higher concentration in whey proteins. Whey proteins are also more similar to human milk, which is why whey proteins are more often known as the replacement for humanized milk production. Another reason as to why caseins are inferior is due to the lower digestion and absorption than found in whey proteins.

In a recent study, protein solubility was measured in the pH range of 2 to 10. A mixture of sodium caseinate and their hydrolysates had minimum solubility at a pH around 4 or 5. They had the highest solubility level in alkalinic pH range, which follows the results of most studies. The results of the study proved that enzymatic hydrolysis improved solubility of their hydrolysates. The increased number of ionizable groups with an increase in hydrophilicity and net charge resulting in hydrolysates promotes hydrolysate-water interaction, thus improving the solubility. The small molecular size also inceases the solubility.

IMF is a major way of knowing whether or not something has a high solubility in water. Remember that, like dissolves like. Using this logic, the polar water would dissolve the most polar protein models. The two main determinants of IMF in a molecule are charge and size. As the charge increases, the solubility increases in water. The smaller the size of the compound, the greater the solubility of the compound in water.

Casein is made of a large amount of residues, which do not interact. There is little structure to a molecule like this. It is also hydrophobic, which makes it less soluble in water. When it is found in suspension in milk for particles, it is held togther by calcium ions. These calcium ions and hydrophobic interactions make up the molecule for casein. The isoelectric point of casein is 4.6. Milk has a pH of 6.6, so casein has a negative charge in milk, so a purified version of casein protein is insoluble in water.

Review of Electrolyte Blog Post by a Nutritionist

Original blog post: http://rackupvitamind.blogspot.com/2012/11/electrolytes.html

If you added this to your blog, it would help get your point across and help add to the content section:

Electrolytes are lost during exercise if one becomes dehydrated. One way to avoid electrolyte imbalance is to drink water during exercise. The amount and frequency needed will depend on the severity of the activity and temperature of the atmosphere. For example, you will require more fluids to remain hydrated if you are exercising outdoors in 80 degree temperatures versus exercising in an air-conditioned gym. As long as you maintain an adequate intake of fluids during exercise, your electrolytes will not become depleted.

However if insufficient fluids are no consumed, and as a result, electrolytes are lost; they will need to be replaced. One quick way is with a sports drink such as Gatorade or Powerade. These are sugar-based drinks that contain sodium and potassium, the minerals that are lost during exercise when dehydration occurs.  The sugar (carbohydrates) in these drinks act as a fuel source for the body. This is beneficial during long endurance exercise, but it will metabolize rapidly and thus require frequent replenishment.  The sole source of energy in these drinks is sugar, and for someone concerned about their sugar intake, they should consider keeping themselves well hydrated with water during their exercise. 

Drinks that contain protein and/or amino acids are not usually meant for consumption to maintain/replace electrolytes. They are frequently consumed, although not necessary, to build/maintain muscle. Someone who consumes an adequate amount of good quality protein in their daily diet will not need to consume supplemental protein drinks. However, if one has a desire to do so, they should make sure that it contains good quality protein composed of 9 essential amino acids.

One easy source of fluids, energy, electrolytes, and protein is milk. Although it is not practical for consumption during exercise due to its microbiological spoilage properties, it is a complete food source to consume after exercising.

Written by Deborah A. Gallucio, M.S., R.D.

Ms. Gallucio received her Bachelor of Science in Foods and Nutrition from Montclair State University and her Master of Science in Nutrition and Public Health from Columbia University.  She is a registered dietitian with the American Dietetic Association and has been in private practice for 31 years.