Biomolecules Flashcards
What are the 4 categories of macromolecules?
Carbohydrates
Proteins
Lipids
Nucleic acids
What bonds carbon forms?
Covalent
What functional groups bind to carbon in different macromolecules?
OH (hydroxyl) in sugars
NH2 (amino) in amino acids
H2PO4 (phosphate) in nucleotides of DNA, RNA, ATP.
What are structural isomers?
Difference in carbon skeleton structure.
What is stereoisomerism?
Difference in location of functional group.
What are enantiomers?
Enantiomers are special types of stereoisomerism.
They are mirror images of each other.
How are polymers made?
Via dehydration
How are monomers made?
Via hydrolysis
What elements macromolecules contain?
Carbohydrates CHO
Lipids CHO
Proteins CHON
Nucleic acids CHONP
What are L and D forms?
The assignments of D and L is used to distinguish between 2 molecules that relate each other with respect to reflection.
L form= left
D form= right
Write information about cellulose.
Found in plants
Subunit is beta- glucose
Bonds 1-4
Unbranched
Write down information about starch (amido).
2 types: amylose and amylopectin
Both are found in plants
Both are made of alpha-glucose
Amylose is unbranched and has bonds 1-4
Amylopectin is branched and has bonds 1-4 and 1-6
Write information about glycogen.
Found in animals
Is made of alpha-glucose
Has bonds 1-4 and 1-6
Is branched (ramificato/ diramarsi) but more branches than amylopectin
What is the structure of proteins?
Central carbon
Amine group
Carboxyl group
R group
How many amino acids exist?
20
Why do we have a diversity of amino acids?
Due to the difference in R group:
Polar/non polar
Charged: negatively (acidic)//// positively (basic)
How do we name amino acids?
Designated abbreviation- valine
3 letters- Val
1 letter- V
What type of bond forms between amino acids?
Peptide bond
What type of ends do proteins have?
N-terminus (amino)
C-terminus (carboxyl)
What are 4 levels of proteins?
Primary
Secondary
Tertiary
Quaternary
What is a primary structure?
Sequence of amino acids in a polypeptide
What is a secondary structure?
Forms beta-pleated sheet, alpha-helix or coil.
This happens because the chain of a.a. In a polypeptide chain has polar covalent bonds within its backbone.
So it folds in a way that hydrogen bonds form between the carboxyl and amine groups.
What is a tertiary structure?
Entire length of amino acids folded into a shape.
Positively charged R groups will bind to a negatively charged R groups.
Polar R groups form hydrogen bonds with other polar R-groups.
Hydrophobic a.a. orientate towards the centre. Hydrophilic a.a. orientate outwards.
R-group of the a.a. Cysteine can form a covalent bond with the R-group of another Cysteine forming a disulphide bridge.
What is a quaternary structure?
Several amino acids sequences linked together.
It also refers to the addition of non-polypeptide components.
