C1: Biological Macromolecules (Ch. 2) Flashcards
Class 1
how are polymers formed? broken?
dehydration synthesis, hydrolysis aka hydration rxn
what is the monomer of proteins?
amino acids
describe the r group of the amino acid glycine. what does it look like?
R= H, very flexible
* SEE INDEX CARDS*
describe the r group of the amino acid proline. what does it look like?
R= secondary amino loop, very rigid
SEE INDEX CARDS
describe the r group of the amino acid cysteine. what does it look like?
R= CH2SH, can form disulfide bridges.
- has terminal sulfur at the end
* SEE INDEX CARDS*
what does methionine look like?
contains sulfur at the beginning (start codon AUG)
* SEE INDEX CARDS*
in a primary protein structure, what are amino acids connected by?
- what does this structure show you?
- are these bonds covalent/ noncovalent? what enzymes can break these bonds?
- this structure is due to what kind of interaction?
- peptide bonds
- the actual sequence of amino acids
- covalent, can be broken by protease and peptidase
- due to backbone interactions
how are polypeptides synthesized?
from the N terminus to the C terminus
what does the backbone of primary proteins look like?
N-C-C
in a secondary protein structure, what kind of bonds are there? what kind of shapes are formed within these structures?
- what does this structure show you?
- this structure is due to what kind of interaction?
- hydrogen bonds
- interactions between amino acid backbones
- alpha helices and beta pleated sheets
- backbone interactions
what is a tertiary protein structure aka?
- what does this structure show you?
- this structure is due to what kind of interaction?
- protein folding
- interaction of its amino acid side chains
- r group interactions
what are the 3 types of non covalent tertiary structure folding?
- nonpolar w nonpolar
- polar neutral w polar neutral
- acidic w basic
what is the type of covalent tertiary structure folding?
cysteine w cysteine, which creates a disulfide bridge
what is the only amino acid that can form disulfide bridges?
cysteine
what is a thiol?
an SH group
what is quaternary protein structure due to?
- what does this structure show you?
- what are 2 examples of quaternary structure? what is the structure of these?
- r group interactions
- interaction of two seperate protein structures
- hemoglobin and immunoglobulin aka antibody. structure is 4 peptide chains connected by quaternary protein structure
what is K-Ras?
a protein made up of amino acid monomers connected by peptide bonds
at physiological pH, what happens to the carboxylic acid part of an amino acid?
- what about the amino group?
- COOH is deprotonated to COO-
- NH2 is protonated to NH3^+
what is the monomer of carbohydrates?
- what is the formula for them?
monosaccharides
- CnH2nOn
what are the 5 important monosaccharides?
- which are hexoses/pentoses?
- glucose
- fructose
- galactose
(hexoses) - ribose
- deoxyribose
(pentoses)
what is the bond of a disaccharide?
- what is the formula?
glycosidic linkage
- C12H22O11
what is sucrose made up of and what kind of carbohydrate is it?
glucose and fructose, disaccharide
what is lactose made up of and what kind of carbohydrate is it?
glucose and galactose, disaccharide
what is maltose made up of and what kind of carbohydrate is it?
glucose and glucose, disaccharide
what polysaccharide provides sugar storage in animals?
glycogen
what polysaccharide provides sugar storage in plants?
starch
what polysaccharide is the plant cell wall made up of?
cellulose
what is the bacterial cell wall made up of?
fungal cell wall?
- peptidoglycan
- chitin
what is the technical name for fat?
triglyceride
what is the lipid bilayer?
hydrophobic interactions made up of phospholipids to make an orderly structure
what is the monomer of lipids?
hydrocarbons in fatty acids (the CH3 and CH2 groups in fatty acids)
what are the characteristics of a saturated fatty acid?
- all single bonds
- saturated w hydrogen atoms
- pack tightly
- solid at room temp
what are the characteristics of an unsaturated fatty acid?
- have one or more double bonds
- kinks in fatty acid chain
- cant pack together well
- liquid at room temp
what is a triglyceride?
- what is its function?
- what is an ex of it in the body?
a fatty acid made up of a glycerol backbone and 3 fatty acid chains
- function is to eat and store fat
- ex is adipocytes aka fat cells in adipose tissue aka fat tissue
what is a phospholipid?
- is it polar/ nonpolar?
- what is its function?
a fatty acid made up of a glycerol, 2 fatty acids and a phosphate group
- amphipathic
- is the main component of membranes
what is cholesterol?
- what does it look like?
- what kind of hormone does it make?
- what is its role in the plasma mem?
a fatty acid made of a tetracyclic ring system
* SEE INDEX CARDS*
- makes steroid hormones
- determines whether plasma mems are rigid or fluid
what is the monomer of a nucleic acid?
- what are the subcomponents of this monomer?
- what is the main ex of this monomer?
- nucleotide
- phosphate, ribose, nitrogenous base. these last 2 form a nucleoside
- ATP
what are 2 important types of nucleic acids?
DNA and RNA
what are the pyrimidines?
cytosine, thymine, uracil
what are the purines?
adenine, guanine
how is DNA synthesized?
- how are the nitrogenous bases paired? how many H bonds do they have?
- how are nucelotides connected?
- 5’ to 3’, antiparallel, complementary
- T to A, 2 H bonds
C to G, 3 H bonds - phosphodiester bonds
what is the sugar of DNA called?
- what is its function?
- how stable is it?
- how long is its lifespan?
- deoxyribose
- genome
- very stable
- long lifespan
what is the sugar of RNA called?
- what are its pyrimidines?
- how does it base pair?
- how is it standed?
- what is its function?
- how stable is it?
- how long is its lifespan?
- ribose
- C and U
- C to G and A to U
- single
- gene expression
- low stability
- short lifespan
what are micelles?
made up of substances that have polar and nonpolar regions (amphipathic)
what is the polarity of inorganic salts?
very polar
enzymes are what kind of macromolecule?
proteins
what kind of macromolecule is insulin?
- describe its structure
- protein
- 2 peptide chains