Exam 1 Flashcards
List the 4 types of biological macromolecules DNE the names of their monomers
Protein
Monomers: Amino acids
Polymer: Polypeptide
Nucleic acid
Monomer: nucleotides
Polymer: polynucleotides
Carbohydrates
Monomer:monosaccharide
Polymer:polysaccharide
Lipid
Monomer: N/A
They are made up of fatty acids
Provide a function of each type of biomolecule
Protein:
Structural
Hormonal
Receptor
Contractile and motor
Defensive
Transport
Enzymatic
Storage
Catalyzing chemical rxn (enzymes)
Carbohydrates:
Structure
Fuel/energy storage
Nucleic acid:
DNA
RNA
Genetic information (transfer): code for protein synthesis
Lipid:
Fatty acids
Used in cell membranes
Hydrophobic
Briefly relate the process of diffusion as a result of thermal motion
Molecules are constantly moving
If the temperature is hot then the molecules start moving faster making diffusion happen faster and when it gets colder they start moving slower making diffusion move slower
Describe the hydrogen bonding present in water
Oxygen- slight negative charge
Hydrogen-slight positive charge
Hydrogen bonds are wea electrostatic interactions
Water is polar and can form hydrogen bond with itself and with solutes
Describe the chemical structure of DNA and RNA
Sugar-phosphate backbones:
5’ end a phosphate is connected
3’ end a hydroxyl group is connected
DNA wraps tightly around Histone proteins to form nucleosmes
Distinguish purines from pyrimidines when shown a chemical structure
Pyrimidines: single ring
Cytosine (C), Thymine (T), Uracil (U)
Purines: double ring
Adenine (A), Guanine (G)
Match base pairs within DNA, RNA, and between the two
DNA
G (3 hydrogen bonds) C
T:::A
RNA
G (3 hydrogen bonds) C
U:::A
Explain how the 3D shapes of different nucleic acids enable their specific functions
DNA double helix: stability, accurate replication, proper gene regulation
RNA has the ability to fold in diverse 3D shapes:
mRNA:
Convey genetic information from DNA to the ribosome for protein synthesis
tRNA:
Has a T shape due to intramolecular base pairing
The shape allows tRNA to carry amino acids acids to the ribosome during protein synthesis and arch its anticodon with the mRNA codon accurately
rRNA:
Folds into complex secondary and tertiary structures to form the ribosomes catalytic and structural core
It allows the ribosomes ability to catalyze peptide bond formation and ensure accurate protein synthesis
Describe the basic components of amino acids and the levels of protein structure
Amino acid:
Carboxyl group
Amino group
Side chain
Primary:
Amino acids attached together with peptide bonded (covalent)
Secondary: hydrogen bonding between peptide backbone atoms
-a helix
-B sheet
Tertiary: held together by side chain interactions with a single polypeptide, 3D
Quaternary: side chain interactions between multiple polypeptides
Recognize key functional groups in biomolecules
Hydroxyl group (OH)
Carboxyl group (COOH or COO-)
Amino group (NH2 or NH3+)
Phosphate group (PO4^2-)
Name the reactions involved in making and breaking polymers
Dehydration synthesis: make a polymer using water
Hydrolysis: break a polymer using water
Identify the role of enzymes in the cell
The lower activation of a chemical rxn which speeds the rxn up
Describe how enzymes bind substrates and catalyze reactions
1.Enzyme binds substrates in active site (lowers activation energy for chemical rxn)
2.Enzyme converts substrate to product
3.Products are released
4. Enzyme isn’t consumed in the rxn
enzymes has one specific substrate and can only catalyze one specific rxn
Contrast competitive and non-competitive inhibitors
Competitive:
Inhibitor competes with substrate for binding to enzyme active site
Can be overcome by adding more substrate
Non competitive:
Inhibitor binds protein outside of active site, causes conformational change that prevents proper enzyme function
Can’t be overcome with more substrate
Describe the conformational change induced by allosteric effectors and
how they alter enzyme function
Allosteric effectors:
Activation-stabilize active form allowing catalysis ( turn enzyme on)
Inhibitors- stabilize inactive form, enzyme can’t catalyze rxn (turn enzyme off)
Molecules bind outside of active site changing overall 3D shape
Explain feedback inhibition in an enzymatic pathway
Allosteric inhibition of pathway enzymes by the products of that pathway
Negative feedback inhibition
Regulating enzymes
Relate cell signaling cascades to changes in enzyme function
Phosphorylation cascade is a common transduction strategy used in cellular signaling pathways
Each phosphorylation event charges target protein shape
Epinephrine signal induces phosphorylation cascade that activated glycogen
Phosphorylate which breaks down glycogen into glucose
