Protein

Protein Sources in Coffiest: 

  • Soy Protein Isolate (21.75 g) 

Amino Acid Profile:

  • Histidine - 0.5 g
  • Isoleucine - 0.94 g
  • Leucine - 1.57 g
  • Lysine - 1.20 g
  • Methionine - .26 g
  • Phenylalanine - 1.0 g
  • Threonine - 0.72 g
  • Tryptophan - 0.26 g
  • Valine - 0.96 g

Conditionally Essential Amino Acids:

  • Arginine - 1.46 g
  • Cysteine - 0.24 g
  • Glycine - 0.8 g
  • Proline - 0.98 g
  • Tyrosine - .72 g

Nonessential Amino Acids:

  • Alanine - 0.83 g
  • Aspartic Acid - 2.22 g
  • Glutamic Acid- 3.65 g
  • Serine - 1.0 g

Protein Sources in Soylent Powder:

  • Soy Protein Isolate (115.5 g) 

Amino Acid Profile:

Essential Amino Acids:

  • Histidine - 2.66 g
  • Isoleucine - 4.97 g
  • Leucine - 8.32 g
  • Lysine - 6.35 g
  • Methionine - 1.39 g
  • Phenylalanine - 5.31 g
  • Threonine - 3.81 g
  • Tryptophan - 1.39 g 
  • Valine - 5.08 g

Conditionally Essential Amino Acids:

  • Arginine - 7.74 g 
  • Cysteine - 1.27 g
  • Glycine - 4.27 g
  • Proline - 5.20 g
  • Tyrosine - 3.81 g

Nonessential Amino Acids:

  • Alanine - 4.39 g
  • Aspartic Acid - 11.8 g
  • Glutamic Acid- 19.4 g 
  • Serine - 5.31 g

Protein Sources in Soylent Drink: 

  • Soy Protein Isolate (22.376 g)

Amino Acid Profile:

Essential Amino Acids:

  • Histidine - 0.51 g
  • Isoleucine - 0.96 g
  • Leucine - 1.61 g
  • Lysine - 1.23 g
  • Methionine - 0.27 g
  • Phenylalanine - 1.03 g
  • Threonine - 0.74 g
  • Tryptophan - 0.27 g
  • Valine - 0.98 g

Conditionally Essential Amino Acids:

  • Arginine - 1.50 g
  • Cysteine - 0.25 g
  • Glycine - 0.83 g
  • Proline - 1.01 g
  • Tyrosine - .074 g

Nonessential Amino Acids:

  • Alanine - 0.85 g
  • Aspartic Acid - 2.28 g
  • Glutamic Acid - 3.76 g
  • Serine - 1.03 g

Protein Sources in Soylent Bar: 

  • Soy Protein Isolate (12.39 g)
  • Oats (9 g)

Amino Acid Profile:

Essential Amino Acids:

  • Histidine -  0.28g; 0.26g via soy,  0.02g via oats
  • Isoleucine - 0.54g; 0.49g via soy, 0.05g via oats
  • Leucine - 0.93g; 0.85g via soy, 0.08g via oats
  • Lysine - 0.71g; 0.65g via soy,  0.05g via oats
  • Methionine - 0.16g; 0.14g via soy, 0.02g via oats
  • Phenylalanine - 0.59g; 0.53g via soy, 0.06g via oats
  • Threonine - 0.42g; 0.39g via soy, 0.03g via oats
  • Tryptophan - 0.15g; 0.14g via soy, 0.01g via oats
  • Valine - 0.57g; 0.51g via soy, 0.05g via oats

Conditionally Essential Amino Acids:

  • Arginine - 0.86g; 0.78g via soy, 0.08g via oats
  • Cysteine - 0.18g; 0.14g via soy, 0.04g via oats
  • Glycine - 0.49g; 0.43g via soy, 0.06g via oats
  • Proline - 0.57g; 0.53g via soy, 0.04g via oats
  • Tyrosine - 0.42g; 0.39g via soy, 0.03g via oats

Nonessential Amino Acids:

  • Alanine - 0.49g; 0.44g via soy, 0.05g via oats
  • Aspartic Acid - 1.3g; 1.2g via soy, 0.1g via oats
  • Glutamic Acid- 2.3g; 2.0g via soy, 0.3g via oats
  • Serine - 0.59g; 0.53g via soy,0.06g via oats

Introduction

A suitable analogy for the roles that proteins play in biology can be found in language.

The Oxford English Dictionary, viewed by many as an authoritative record of the english language, contains 600,000 entries. Each entry describes the function and role of a specific combination and arrangement of letters - more commonly known as, "words."

Every word has a specific purpose in language. "Because" indicates that an explanation of a topic is about to follow. "Science" describes the systematic study of a subject, executed through observation, hypothesis and experimentation.

Despite the incredible breadth and diversity of words, as an alphabetic language, each english word is formed from the same set of 26 letters (Wow!).

In the "language" of human biology, proteins play the role of words. There are tens of thousands of different proteins in the body. In fact, the average eukaryotic cell has the ability to make roughly 30,000 different proteins.[1]

Similar to words in an alphabetic language, in human biology, all proteins are made from an "alphabet" of 20 amino acids.[2][3] 

Nutritional Role

When protein is ingested, it is catabolized, or broken down, into its disparate amino acids.

Of these amino acids, nine are not produced by the body and are thus essential.[4] Six of the twenty amino acids may not be produced in adequate quantities in certain physiologically stressful conditions.[5] Infants of low birth weight, for example, can't synthesize enough cysteine and proline.[6] Five amino acids are considered nonessential because they are naturally synthesized in the body.[7]

Unlike words in a language, proteins eventually decay and break down. The time from when a compound is produced until it decays to half of its initial quantity is called its half-life. The average half-life of protein can range from 0.9 days for liver tissue proteins, to 4.6 days for proteins in brain tissue, and all the way to 10.7 days for proteins in muscle tissue.[8] Once there is a need for a specific type of protein, a cell will automatically start to produce it via a process called protein synthesis.[9]

Types of Protein

Like words in a language, there are thousands of different types of proteins. Proteins vary wildly in shape and size. Cytochrome complex, a protein associated with a cell's mitochondria, consists of 104 individual amino acids. Titin, a protein found in muscles, is made up of 26,926 individual amino acids.[10] The incredible diversity in the structure of proteins assists with nearly every metabolic pathway, and ultimately makes life possible.  

Hemoglobin, a transport protein, distributes oxygen from the lungs throughout the body. Immunoglobulins, also known as antibodies, are defensive proteins and disrupt the activity of viruses or bacteria by binding to their available receptor sites.

Insulin, a hormonal - or chemical messenger of sorts - protein, regulates blood sugar concentration by causing cells to absorb glucose. On the outside of a cell, insulin interacts with insulin receptor proteins, which pass along insulin's "message" to the inside of the cell.

Enzymes, which are made of proteins, make it easier for specific chemical reactions to occur by reducing the minimum amount of activation energy needed.

Ferritin is an intracellular storage protein that maintains reserves of iron. Actin and myosin are motor proteins which enable muscles to contract. Elastin is a structural protein found in connective tissue that allows the tissue, like elastic, return to its normal shape and size after being stretched.

Fundamentally, proteins are the words through which DNA expresses itself and are the mechanism by which DNA controls the complex processes within the human body.

 

 


[1] Nelson, David L., Michael M. Cox, and Albert L. Lehninger. "Principles of Metabolic Regulation." In Lehninger Principles of Biochemistry, 588. New York: W.H. Freeman, 2013.

[2] Certain amino acids have additional roles including translation and transcription regulation (Leucine), enzyme activity regulation (phenylalanine) and as a neurotransmitter (glutamate, tryptophan), among others.

[3] Erdman, John W., Ian MacDonald, and Steven H. Zeisel. "Protein and Amino Acids." In Present Knowledge in Nutrition, 70. Washington, DC: International Life Sciences Institute, 2012.

[4] Essential amino acids: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine.

[5] Conditionally essential amino acids: arginine, cysteine, glutamine, glycine, proline, tyrosine.

[6] Pencharz, P. B., J. D. House, L. J. Wykes, and R. O. Ball. "What Are the Essential Amino Acids for the Preterm and Term Infant?" Recent Developments in Infant Nutrition 9 (1995): 278-96.

[7] Nonessential amino acids: alanine, aspartate, asparagine, glutamate, serine.

[8] Nelson, David L., Michael M. Cox, and Albert L. Lehninger. "Principles of Metabolic Regulation." In Lehninger Principles of Biochemistry, 590. New York: W.H. Freeman, 2013.

[9] Khan Academy has an excellent overview of transcription and translation - the fundamental components of protein synthesis.

[10]  Nelson, David L., Michael M. Cox, and Albert L. Lehninger. "Amino Acids, Peptides, and Proteins." In Lehninger Principles of Biochemistry, 87. New York: W.H. Freeman, 2013.