Amino Acid Video Review

 

This is a video review on Amino Acid Structure By Tracy Kovach from YouTube. I personally like this video because it is short and gets right to the point and pretty much covers all the necessary information.

In this video Tracy talks about what amino acids do and how they can be illustrated. She starts off by talking about the hemoglobin protein and explains how its job it to pretty much taxi around oxygen by picking it up from the lungs and dropping it off to the tissues where it is needed in the human body. The cells in the tissues then use the oxygen to create ATP, which is needed for all the metabolic processes for life. She then explains how amino acids are the building blocks of the protein hemoglobin and how without them this process would not be able to occur and we would therefore not be able to live.

She goes on to explain the structure of an amino acid. In an amino acid there is and amino group, the carboxylic group and the alpha carbon atom/chiral carbon that links the amino and carboxylic group. A hydrogen atom is connected to the alpha carbon as well as a side chain/R-group. A chiral carbon is a carbon that has four different groups attached to it. The only amino acid that does not possess a chiral carbon is Glycine. Glycine is the simplest amino acid with a R-group of only Hydrogen. Tracy then draws the Fischer projection – an illustration of an amino acid that highlight the four groups surrounding the chiral carbon – of two amino acids. There are two different types of Fischer projection configurations L-Amino Acids and D-Amino Acids. Whether the projection is L or D depends on where the amino group is. If the amino group is on the left it is L and if it is on the right it is D. L and D amino acids are enantiomers, meaning they are mirror images of each other however they can not be superimposed on one another. They are pretty much like your hands. Your hands are mirror images but if you place one on top of the other they would lay differently.

*Fact: L-amino acids are the only configuration found in the human body.

Well that is all for this video review I hope you enjoyed! Remember to subscribe to Tracy Kovach on YouTube!

Chao for now!

 

N-Zymez homie!

What the heck are enzymes?

You don’t know what enzymes are? Really?! Ok that’s fine. An enzyme is simply a biological catalyst. It speeds up a biological reaction with out being used or changed and it is specific, meaning each enzyme only works on a specific substrate. For example lipase hydrolyses lipids and only lipids. (How do enzymes speed up reactions though? ) OMG glad you asked! They just create a different pathway that has lower activation energy than the original pathway.

Most enzymes are proteins, some are RNA molecules known as ribozymes (they satisfy mostly all of the enzymatic criteria eg. they are substrate specific, they speed up the reaction rate, and they remain unchanged after the reaction. Some antibodies have catalytic properties and these are called abzymes.

What’s the big deal about enzymes?

Without enzymes life is literally impossible! Enzymes allow for respiration to occur. Which means, no enzymes à no energy à no life. Thank goodness for enzymes right? Yeah… trust me I know.

According to Ask.com, in the human body approximately 2700 enzymes can be found. These enzymes are separated into three major groups, which are: metabolic enzymes, food enzymes and digestive enzymes. Their location in the body depends on their function. Enzymes can be found in the mouth in saliva, in the stomach and everywhere else in the body. Without enzymes we are nothing!

This is an energy profile diagram.

This diagram shows exactly how enzymes speed up the reaction to produce product.

But what is activation energy? Activation energy is the minimum energy needed for a reactant to react.

How do enzymes get their name?

Um… their parents obviously name them at birth just like everyone else! No, just kidding. Enzymes are either named based on the substrate they react on, the action they perform, they end in ‘ase’ or they just have some random name that has nothing to do with them. Because names were getting out of hand, our homies at The International Union of Biochemistry and Molecular Biology, IUBMB for short, decided to come up with a naming system. They divided the enzymes into 6 classes. In each class is a sub class and in each subclass there is a sub-subclass. Each is numbered and therefore a series of 4 numbers specifies a specific enzyme (this is called the Enzyme Commission [E.C.] number.

The 6 major classes are: 

1. Oxidoreductases – Catalyze oxidation-reduction reactions
2. Transferases – Catalyze the transfer of C,N or P containing groups
3. Hydrolases – Catalyze cleavage of onds by adding water.
4. Lyases – Catalyze clevage of C-C, C-S an some C-N bonds
5. Isomerases – Catalyze isomerizaton of optical or geometric bonds
6. Ligases – Catalyze the formation of bonds between C and O, S, and N couples to hydrolysis of high energy phosphates.

Holoenzyme?? Hol up.. holo what??

Omg chillllll! Its simple! A holoenzyme is just a biochemical compound that is a combination of an enzyme and a coenzyme. And before you go a-wall!  A coenzyme is just a substance that is necessary for an enzyme to function.

Inorganic Catalyst v.s Biological Catalyst

Well incase you didn’t know, biological catalyst are THEE (emphasis on thee) fastest by far when compared to inorganic ones. Biological catalysts are also the most efficient. For example: during the Haber process, which makes ammonia, the temperature needed is 450 degree Celsius, at 1000 atm! What? Amylase breaks down starch to maltose in my mouth and at less than 100 degrees Celsius! And unless you’re a fire-breathing dragon it does the same for you!

So whenever you’re feeling on top of the world, and feel that you can take on a lion, tiger or bear… give enzymes a quick shout out, because with them my good friend… you are without life.

Here’s some pickup lines! Use them wisely.

In that order!

Chao for now!

“Title about Protein”

 

So, last week we discussed Amino Acids… now, let’s be blunt, let’s be quick, let’s talk PROTEINS.

Protein Structure: There are four levels of protein structures and those are as follows
v  Primary

v  Secondary

v  Tertiary

v  Quaternary

But, what determines these levels of protein structure?
Who says polypeptide chains? Who says the linear sequence of amino acids? Who says both? Well I obviously don’t know who said what, but if you said both, you’re right!

Now let’s talk about how the levels are determined…

 

 

 

 

RECAP!!

As blogged before, the bond between two amino acids is called a peptide bond.

Peptide bonds are formed removing a water molecule from two different amino acids. The sequence of amino acids determines the positioning of the different R groups and this positioning determines the order in which the proteins fold and essentially the structure of the molecule.

PRIMARY STRUCTURE:

The linear sequence of amino acids that make up the polypeptide chain is determined by the genetic encoding of the sequence of nucleotide bases in the DNA.

 

SECONDARY STRUCTURE:

 

This is the regular folding of regions of the polypeptide chain. Two of the most common types of ‘protein folds’ are called the α – helix (coiled) and the β pleated sheet;  which is folded.

Compared to other conformations, the α-helix if formed more readily due to its optimal use of internal hydrogen bonding.

 

 

 

The Hydrogen bonding in the secondary structure occurs between atoms in the peptide bond

TERTIARY STRUCTURE:

Tertiary… this is a three dimensional structure and is formed by the twisting of the polypeptide chain. The linear sequence of amino acids is usually folded into a compact structure and becomes stable by many non-covalent interactions between the side groups of the amino acids.

 

QUARTERNARY STRUCTURE:

Not many proteins reach to this stage of folding (protein structure) but one example of a protein that has the structure is Haemoglobin. This structure is formed by the combination of more than one polypeptide chain. Interactions between them are; ionic, disulphide, hydrogen bonds and hydrophobic (not afraid of water, but rather ‘water hating’) interactions.

 

 

 

RANDOM FACTS ABOUT PROTEINS.

• About 18-20% of the body’s weight is protein.

 

• Hair is made up of a protein called keratin, which forms a helical shape. It contains sulphur bonds and so the more sulphur links present, the curlier a person’s hair can be. (I LOVE CURLS)

 

• Protein is a macronutrient; these provide calories/energy and are essential for survival.

 

• The lifespan of most proteins lasts two days or less.

 

• Without Albumin, the human body would begin to swell. (When I think of Albumin, I think of eggs.. when I think of eggs, I think of PROTEIN)

 

• Protein in semen acts on the female brain to prompt the ovulation process. #fertilize #dontgetideas #okaygetideas

 

• Errors in protein function can cause diseases such as Alzheimer’s and cancer.

 

•  The body needs protein to grow, heal, and carry about nearly every chemical reaction in the body.

 

• Complete or Whole Proteins contain all nine of the essential amino acids.

 

• Insufficient protein in diets can prohibit weight loss.

 

 

References:

Pictures

http://www.vitalityfitnesscalgary.com/protein-4-reasons/

http://www.slapcaption.com/josh-nichols-weight-loss-success/

http://hanguyenbiologyhlblog.blogspot.com/2013/01/proteins-homework.html

 

Information

http://www.bodybuildingpro.com/proteinrating.html

http://www.nature.com/horizon/proteinfolding/background/disease.html

http://www.youtube.com/watch?v=ZWLNkEJloJA&feature=youtu.be

 

 

 

AMINO ACIDS AND PROTEINS!

CALL ME ACID…… AMINO ACID *brings in intro music*

Amino!!!!!!! I think I’ll name my daughter that. Anyways, onto the topic of amino acids and proteins. Amino acids are the initial structures for one of the most important biological compounds out there i.e. PROTEINS. Proteins have many functions in the world we live in today that we know of and don’t know of. To generalise, some of these functions include receptors, channels, transport, enzymes, storage, structural and immune response. Let go a bit deeper into the biochemistry of the building blocks which make up proteins, i.e. amino acids.

 

ALL THAT R GIRL!!!!!!!!!!

Soooooooooo….. If I show you a Fischer diagram of a molecule, how would you know if it’s an amino acid or not. What’s that? You don’t know? Well I’m not shockedJ.  In my own words, an amino acid can be described as an α carbon bonded to four different groups. But not just any four groups. The four groups must be a hydrogen atom, a carboxylic group, an amino group and a R group.

 

 

Another question: So how can we distinguish between the different amino acids?

Answer: Via the R groups of course.

What makes each amino acid different is the R group. The R group can range from very small for example Glycine (smallest amino acid) to very large e.g.  Tryptophan (largest standard amino acid). The R groups can be split up into different categories.

1. Non polar, aliphatic R groups e.g. Glycine.
2. Polar, uncharged R groups e.g. Serine.
3. Aromatic R groups e.g. Tyrosine
4. Positively charged R groups e.g. Lysine
5. Negatively charged R groups e.g. Glutmate.

 

 

AMINO ACID ABBREVIATIONS

The names of some amino acids can be abbreviated for the purpose of ease. Here is a chart showing some names and abbreviations which can be a three letter code or a one letter code.

 

 

MARRIAGE OF CYSTEINE 

When two cysteine molecules react with each other, they go through an oxidation reaction where they lose hydrogen. A bond between the sulphurs in the molecules form. This bond is called a disulphide linkage and the new molecule is called cystine. A reduction reaction can take place in cystine where hydrogen is gained and the two cysteine molecules are reformed.

 

 

ZWIT ZWIT

Amino acids can exist in the non-ionic form and also the zwitterionic form. It is quite easy to explain how one changes to the other. A proton/hydrogen from the carboxylic group adds itself to the amino group to form the zwitterion. The carboxylic group will now have a negative charge and the amino group will take a positive charge.

 

 

DON’T GET IT TWISTED (Ninhydrin reaction vs Biuret’s test)

Did you know that amino acids are colourless? So how do we know they a part of a substance? We test for them….DUH!!!!!!!! But which test do we use? Ninhydrin or biuret? C’mon, are you for real bro? We use Ninhydrin which ONLY test for amino acids and not proteins. Biuret’s test works on proteins ONLY!!!!! In the ninhydrin test, if a purple colour is observed, then the test is positive for AMINO ACIDS. In the biuret’s test the same purple colour means that the test is positive for PROTEINS.

 

 

PEPTIDE BONDS!!!!!!!!!!

These are the bonds created between amino acids. When two amino acids react, the carboxylic group of one amino acid reacts with the amino group the other amino acid to form a covalent bond called a peptide bond. The two amino acids joined together are now called a dipeptide. The reaction is a condensation reaction meaning that water is given off.