Salut! Hola! Hi! Namaste! Yow wa ah gwaan! Oppa trini style??

So many ways to greet right? I’ve decided to make this reflection a little interesting. No formal English! We doing this TRINI style! So basically what I’ve created is a short dialogue between two friends Mindy and JayJay to explain a really interesting protein fact 🙂

At home in the living room where Mindy is reading the newspaper

Mindy: Jay bwoy ah readin dis paper here but i cetchin meh skin tuh see! I seein d ting cloudy cloudy. Way yuh put meh glasses?

Jay: *laughs* well look who gettin ole now. like yuh hav cataracts like granny and ole brownie from up d road

Mindy: Cataracts yuh say? Naaaaa man! D print on dis ting jus to fine! Buhhh Jay you talkin bout cataracts…u kno wa dat really is?

*SILENCE*

ohhh I thought so

Jay: Well amm all i kno is ole people does get it n ting

Mindy: Well let me explain it tuh yuh! Cataracts is really caused by d denaturation of proteins in d lenses of yuh eye! First up to make it simple for yuh, it is a cloudin of the lens of the eye!

Jay: We have proteins in we eye?

Mindy: YESS! So u din kno we eye is mostly water and protein? It does help with d len’s structure and flexibility.  D protein is arranged in a specific way that keep d lens clear and it does allow light tuh pass tru it to focus a clear image onto the retinal surface. As we geh older, some of d protein may clump together an start tuh cloud a small area of d lens. Dis is d reason y everybody tink only ole people does get cataracts. Over some time, d cataract may become more dense or cloud more of d lens, making it more difficult tuh see tru. Sooo yuh understan wa i talkin bout?

Jay: Yeaaa i din kno it was about all of dat

Mindy: Yes, proteins have a specific shape that does help d molecules participate in chemical reactions! Denaturing does happen when that shape is compromised n d molecule can no longer function to d best. But i go call u later to explain some more things na. Meh modda callin meh! I sure I hadda travel home! We go pick up!

Jay: Aite we go link! Thanks for d info eh!

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WELLL talk about broken English lol! Just a fun way to share an interesting fact! 🙂 This week was a bit tough for me since blogs and labs were due and midterms are still running. 😦 In class, we focused on topics like cholesterol, sphingosine, nucleic acid and nucleotides. It was a long week but Friday is almost here! 

The general structure of Sphingosine can be seen in the fig. below

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It is an 18 carbon molecule, has a double bond between carbons 4 and 5, has a hydroxyl group on carbons 1 and 3 and an amino group on carbon 2.

Well I hoped everyone enjoyed this post! That’s all for now folks! aka Dais it until ma next post :p 😉

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INTERESTING FACT for my fellow curly haired peeps! ;)

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On the hot seat is Mr. Protein! For this reflection, I’ll be sharing something interesting, especially for ma curly haired peeps! Hair is made up of a protein, keratin, which forms a helical shape. This protein has sulfur bonds, and the more sulfur links it has, the curlier a person’s hair will be! ie a hair shaft with more sulfur ions placed closer together will result in a tighter curl pattern. Having curly hair can be a stress at times! Frizz is a major problem lol! Once in a while I’m guilty of using a flat iron even though I hear ‘too much heat is bad for your hair.’  There are 3 types of bonds in our hair,hydrogen, salt and disulphide bonds! Heat loosens the hydrogen and salt bonds which causes a change in hair texture and therefore results in a straighter pattern!

Shoutout to those with curls! 🙂

Don’t forget to check out my Fun Facts Page for more interesting stuff! 😀

Quote for this week——> “Whatever else there may be in our nature, responsibility toward truth is one of its attributes.” — Arthur Eddington 

Have a great week! 

A look back at today

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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).

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Photo credit- http://www.ucl.ac.uk/~sjjgsca/protStructTable.gif

Let’s take a look at Primary, Secondary and Tertiary Structures…

 Primary StructureThis 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 StructureThis 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