FoB Lecture 3 - Biomolecules

What are the 4 biomolecules?

proteins, carbohydrates, nucleic acids, lipids

Biomolecules are ____ built of ______ subunits.

polymers, monomer

What is the backbone of all biomolecules? what is the molecular % of cells?

carbon

70% water and 30% other chemicals

How are monomers connected (bond)?

What is the name for the connection of monomers? What does the process look like?

covalent bond

dehydration/condensation - joins monomers together to build a polymer by requiring energy input release H2O as a byproduct

Biomolecules are polymers of monomer subunits.

What are the monomers that build each polymer?

Which is not a polymer?

carbohydrates - monosaccharide (simple sugar)

protein - amino acid

nucleic acid - nucleotide

not - lipid

Carbohydrates: 2 shapes and importance

can be ringed or linear

Alpha-1,4 and alpha-1,6: branched carbs (store energy)

Alpha-1,4: linear (provide structure)

Monosaccharides are joined together by _________ (_______) to form polysaccharides

What is the name for this bond and how are they bonded?

Condensation (dehydration) - energy in and water out

glycosidic bond - covalently

Carbohydrates: define these terms

Disaccharides:

Oligosaccharides:

Polysaccharides:

glycoprotein:

Disaccharides: two monosaccharides linked by covalent bonds

Oligosaccharides: 3-20 monosaccharides

Polysaccharides: hundreds or thousands of monosaccharides

glycoprotein: protein with carbohydrates

Proteins - monomer, function, important functions (2)

monomer: amino acids

function: store energy, provide structure, and serve as cell identity markers

information for their assembly held in DNA, shape important for function

what is the indicator word for protein?

what kind of bond forms between two monomers and how?

peptide

peptide bond - OH bonds to O and needs E / releases water to form bond

what functional groups make up an amino acid monomer? draw it

amino group, “R” reside side chain, carboxl group

what order are proteins written and synthesized in?

N-terminus to C-terminus

What are the 3 major groups of amino acid side chains?

electrically charged (acidic/basic)

polar

nonpolar

What determines which group an amino acid belongs to?

the chemical properties of its R-group (side chain)

what makes a side chain electrically charged? what are the two types?

it has an overall + or - charge ; acidic - and basic +

what makes a side chain polar?

it has partical charges but no overall charge

what makes a side chain non-polar?

little / no charges separation, often mostly C-H

what side chains can form hydrogen bonds? van der waals?

charged and polar

all

what interactions are important for charged side chains?

ionic interactions + hydrogen bonds

what interactions is important for polar side chains?

hydrogen bonds

what interactions is important for nonpolar side chains?

van der waals and hydrophobic interactions

There are __ levels of structure.

4

What occurs in the primary level (1) of protein structure? Stabilized by?

Order of amino acids (monomers) in a polypeptide stabilized by peptide bonds

What is a residue? What step in the folding process is residue order important?

Amino acid - residue order is important for 2,3,4

What occurs in the secondary level (2) of protein structure? due to what type of bonding?

interactions between backbone (amino/carboxyl)

hydrogen bonds along the peptide bonded backbone

What are the 2 distinct patterns/structures?

Alpha helix (right-handed coil resulting from hydrogen bonds

Beta-pleated sheets (two or more polypeptide chains are aligned after 1 big turn; hydrogen bonds between chains

What occurs in the tertiary level (3) of protein structure? stabilized by

2nd step of 3-D folding - R-SIDE CHAIN INTERACTIONS

• interactions between R groups - stabilized by disulife bridges, van der waals, ionic bonds, and hydrogen bonds

What occurs in the quaternary level (4) of protein structure?

shape is produced - interactions with other polypeptides bond together - final function form of a protein

Why do each subunit have its own tertiary structure in the proteins level of structure?

due to interactions with protein subunits by hydrophobic reactions, van der maals, ionic bonds, and hydrogen bonds

proteins must be folded correctly into a specific, 3 dimensional shape to function. t/f

true

what happens when a protein is denatured? can it refold?

loss of 3d structure, loss of function

can refold if correct conditions are met again

what causes a protein to denature?

heat, pH, salt, solvents

what is a prion and what can it cause?

misfolded proteins and disease

cause other proteins to misfold

nucleic acids - monomer, function, important functions (2)

monomer: nucleotides

function: DNA stores info for making proteins - many jobs

What do nucleic acids form? What order are they built in?

important molcules in monomer form (ATP, AMP, GTP)

have 2 distinct ends (poles) and are built in the 5’ to 3’

what type of bonds join nucleotide monomers and nucleic acids?

phosphodiester - covalent

What makes up the nucleic acids?

nitrogenous base, phosphate , pentose sugar backbone

what is DNA function? form?

stores information to make proteins

left handed double helix

what is RNA function?

uses DNA to make proteins, enzyes, genegulatory units, signaling, ect

what are the 2 pairs for DNA?

adenine - thymine

cytosine - guanine

what are the 2 pairs for RNA?

adenine - uricil

cytosine - guanine

nucleic acids store the information for making proteins ___ and carrying out proten synthesis ___

DNA , RNA