Learning is an experience…hmm! When it comes to the actual test, many of us forget what was thought to us or what we studied. Guilty over here! *shame face* I am one of those avid crammers! Trust me it’s no good because right after the exam you completely forget everything you’ve learnt because that’s the way you trained your brain to work However, I’ve learnt how to actually study in advance for an exam. Once you make time to go through your work and not cram you’ll eventually remember stuff and it’ll become natural. Ok, let me get to the point! Studying could be boring lol but there are different methods you could use. For example, say I had to remember the amino acids Alanine, Glycine, Leucine and Serine, I’ll use something like ‘All Girls Love Shopping‘. The 1st letter of each word would correspond to each amino acid respectively. There are tons of other methods to help you remember stuff!
Check out this song to remember amino acids! Kudos to this guy!
Credit goes to Jeremy Ying and his youtube channel! http://www.youtube.com/channel/UCN_KSElNBjZVzhvsnI6mH2g?feature=watch
What’s cracking cyber people! lol… ok i did NOT think about that picture when i asked that question :p Today in Biochem1362 we focused on the structure of Proteins.
PROTEINS (Macromolecules) are made up of monomers (amino acids).
Photo credit- http://www.ucl.ac.uk/~sjjgsca/protStructTable.gif
Let’s take a look at Primary, Secondary and Tertiary Structures…
Primary Structure– This is the order of the amino acids of which the polypeptide chain is made up of. The only bonds are covalent bonds between sucessive amino acids. Proteins differ in the variety, number and order of their constituent amino acids. The sequence of the amino acids in the polypeptide chain is controlled by the coded instructions stored in the DNA of the chromosomes in the nucleus.
Secondary Structure– This is the way in which the amino acid folds itself as a result of hydrogen bonding. There are 2 types, α helix and β pleated sheet.
A polypeptide chain often coils into an α helix. The helix is held in shape by attraction between the O2 of the CO group of 1 amino acid and the H of 1 amino acid four places ahead of it. This twists the chain into a spiral (helical form) where the twists are kept in place by hydrogen bonds. A small portion or the whole polypeptide chain can twist into an α helix. Eg. Keratin, an example of an insoluble protein found in nails. In β pleated sheets, protein strands lie adjacent to each other. H bonds form from the interaction of different chains resulting in a flat structure that becomes folded like a sheet. Eg of such protein is silk
Tertiary Structure– This is the precise 3Dshape that is unique to proteins and rises when the molecule is further folded and held in a particular complex shape. This shape is made permanent by four different types of bonding (ionic, hydrogen, hydrophobic, disulphide linkages) between adjacent parts of the chain.
That’s a wrap for now!
Thought for today! 😉
Other sources- http://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb1/part2/protein.htm
Thank God it’s Friday is probably what most of us are saying! Yep, I’m guilty although I had Monday and Tuesday off. ‘I have too much free time’ said no one ever lol! This week was surprisingly a bit more on the chill side for me. Biochemistry…I had one lecture for the week and we went through our Carbohydrates quiz and we did some more work on proteins and amino acids. I’m not gonna lie, I’m actually enjoying this topic thus far! I know for sure I prefer it over carbs any day! :O
So let’s see, there are about 20 amino acids that are needed and essential for life! These are known as standard amino acids. Our bodies only produce 11 of these. The other nine is obtained through food since our bodies cannot synthesize them. In a cell, ribosomes are responsible for protein synthesis.A lack of any amino acid, would therefore be a limiting factor in protein synthesis. Eukaryotes are able to make these shortage of amino acids from other substrates. Quite interesting huh!
Let’s take a look at Leucine!
Photo credit – http://www.chem4kids.com/files/aminoacids/art/leucine.gif
This type of amino acid is nonpolar and is one of those not synthesized in our bodies.It is also, like valine a branced chain amino acid. It can be found in protein foods such as fish, poultry and sesame seeds. Because of it’s ability to easily convert to glucose, leucine aids in blood sugar regulation. Bodybuilders, also have a high intake of this amino acid because it influences muscle protein metabolism!