(2) Molecular Biology Flashcards
Outline the number and type of bonds carbon can form with other atoms
Carbon can form up to four bonds that are covalent
List the four major classed of carbon compounds used by living organisms.
Carbohydrates, lipids protein and nucleic acids
Define metabolism and catalysis
Metabolism: chemical reactions in the body’s cells that convert food to energy
Catalysis: when a substrate speeds up a chemical reaction without being personally altered.
Define metabolism and catalysis
metabolism: chemical reactions in the body’s cells that convert food to energy
catalysis: when a substrate speeds up a chemical reaction without being personally altered
Define monomer and polymer
monomer: molecule of any class of compound, mostly organic, can react w other molecules to form large molecules
polymer: molecule of a class of natural/synthetic substances composed of very large molecules called macromolecules.
State the role of enzymes in metabolism
Enzymes speed up biochemical reactions by facilitating thee molecular rearrangements that support cell function.
Describe condensation reactions
Dehydration synthesis
two molecules condense and a water is lost to form a large molecule.
Contrast anabolism and catabolism
ANA: use energy, synthecization
CATA: release energy, breaking down molecules
Contrast anabolism and catabolism
ANA: use energy, synthecization
CATA: release energy, breaking down molecules
Describe hydrolysis reactions
Molecule of water breaks chemical bond(s)
Explain the role of urea in the falsification of vitalism
Vitalism suggests that an organic molecule such as urea cannot be synthesized solely from inorganic sources. It was believed that synthesis of urea required a living organism or some part of a living organism, such as a kidney.
Parts of an atom
neurons, protons, electrons, nucleus
Contrast ion and atom
ION:
- electrically charged
- different number of protons and electrons
- may contain 1+ atoms
ATOM:
- electrically neutral
- same number of protons and electrons
- number of protons defines element
define anion and cation
an: negatively charged
cat: positively charged
contrast covalent, ionic and hydrogen bonds
covalent: atoms bound by a shared electron(s)
ionic: atoms bound by oppositely charged ions
hydrogen: weak chemical bond where a hydrogen atom and and electronegative atom bond
molecular formula for water
H2O
Cause and effect for the polar nature of water
cause: oxygen has a greater pull on electrons then hydrogen
effect: unequal sharing of atoms
describe where and how water is able to form hydrogen bonds
water forms hydrogen bonds between the partial positive hydrogen of one water molecule and the partial negative oxygen of another molecule.
contrast adhesion with cohesion
adhesion: ability to differentiate molecules to stick together
cohesion: ability for some molecules to stick together
outline an example of the cohesive property of water being of benefit to life
water cohesion means a high heat capacity
Outline a benefit to water’s high specific heat capacity
Large bodies of water take a lot of energy to heat, stay more constant, protect wildlife
Outline a benefit to water’s high boiling point
Helps to keep it in liquid form for most biological processes.
Explain why water is such a good solvent with a variety of substances
Because of its polarity and ability to form hydrogen bonds
List the types of molecules water will dissolve
Ions and polar molecules because they are hydrophilllic
Non-polar and non-ionic molecules are (hydrophilic/hydrophobic)
hydrophobic
Polar and Ionic molecules are (hydrophilic/hydrophobic)
hydrophilic
Compare the physical properties of methane and water
WATER: solvent properties/polarity of water = many substances can dissolve in it
METHANE: non-polarity = weak dispersion forces
Explain sweating as a mechanism to cool the body
heat of vaporization
excess body heat is used to convert beads of sweat into vapor, you start to cool down
State if the following molecules are hydrophilic or hydrophobic
Glucose
Amino-Acids
Cholesterol
Fats
Oxygen
Sodium Chloride
Glucose =hydrophilic
Amino-Acids =hydrophobic
Cholesterol =hydrophilic
Fats =hydrophobic
Oxygen =hydrophilic
Sodium Chloride =hydrophobic
Define monosaccharides, disaccharides and polysaccharides
mono: single sugar molecule
glucose, fructose, galactose
di: double sugar molecule
sucrose, maltose, lactose
poly: long changes of sugar molecules
cellulose, glycogen, starch
explain a condensation reaction from connecting to monosaccharides to form a disaccharide
Carbon #1 of glucose A binds to Carbon #4 of glucose B
Describe the differences between saturated and unsaturated fat (mono- / poly-)
Saturated fat lacks double bonds between individual carbon atoms
Describe the difference between cis and trans fatty acids
Cis: naturally bent
Trans: artificially modified
Explain a condensation reaction connecting fatty acids to glycerol to form a triglyceride
Hydroxyl groups of the glycerol combine with the carboxyl groups to form the fatty acid
State the structural difference between alpha and beta glucose
difference in position of OH groups
Explain the energy storage of lipids compared to that of carbohydrates
Lipid molecules contain more energy/gram then carbohydrates
Outline the effects of a BMI that is too high or low
High: The higher your BMI, the higher your risk for certain diseases such as heart disease, high blood pressure, type 2 diabetes, gallstones, breathing problems, and certain cancers.
Low: compromised immune function. respiratory disease. digestive diseases.
State the relationship between enzyme substrates and enzyme products
substrate + enzyme = product
Explain the relationship between enzyme structure and enzyme specificity, including the role of the active site
Specificity results from shape because only the side chains of the enzyme change shape and bond to the active site
Explain the role of random collisions in the bindings of the substrate with the enzyme active site
Successful collisions are ones in which the substrate and active site are correctly aligned to allow binding to take place
Explain the role of random collisions in the bindings of the substrate with the enzyme active site
Successful collisions are ones in which the substrate and active site are correctly aligned to allow binding to take place
Describe the induced fit model of enzyme action
A substrate binds to an active site and both change shape slighty
Describe the lock and key model of enzyme action
the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another
Explain how temperature affects the rate of enzyme activity
At too low of a temp, molecules slow down. At too high, molecules denature
Explain how pH affects the rate of enzyme activity
Best when in between acidic and alkaline
Explain how substrate concentration affects the rate of enzyme activity
increase in substrate = increase in the rate of enzyme catalyst reactions
What is the relationship between substrate concentration and enzyme activity?
More substrate = more activity
State the effect of denature on enzyme structure & function
denature causes protiens to be disfunctional
State the source of the lactase enzyme used in food processing
a type of yeast in milk
State the reaction catalyzed by lactase
lactose → glucose and galactose
Outline three reasons for using lactase in food processing
- allows lactose intolerant people to consume dairy
- galactose and glucose are smoother and sweeter to consumer
- shortens production time
Describe polypeptide chain formation in terms of the formation of peptide bonds and condensation reactions
AN -OH from the carboxyl on one amino acid combines w an -H from the amine of the other amino acid. The -H and -OH combine to form water. A peptide bond is formed with a C-N bridge between the two amino acids.
Determine the number of peptide bonds given the number of amino acids in a polypeptide
of amino acids - 1 = # of bonds
State the number of amino acids used by living organisms to make polypeptides
20
Outline the relationship between genes and polypeptides
3 genes = 1 amino acid
DNA → RNA → Ribosome → Polypeptide
Contrast proteome with genome
genome= all DNA
proteome = all protiens
Define denaturing
Taking away the quality of
State the two types of nucleic acids
DNA: deoxyribonucleic
RNA: ribonucleic
Explain how nucleotides can connect to form a nucleic acid polymer
nucleotides connect by creating covalent bonds between the sugar of one nucleotide and the phosphate group of another nucleotide in a condensation reaction
state the names of the nitrogenous bases found in DNA and RNA
cytosine, thymine (DNA only), guanine, adenine, uracil (RNA ONLY)
Compare the structure of DNA and RNA
DNA: deoxyribose, double-stranded, A, G, C, T
RNA: ribose, single-stranded, A, G, C, U
Define antiparallel in relation to DNA structure
adjacent molecules are oriented parallel to each other but in opposite directions. In DNA one strand runs 5’-3’ and the complementary strand runs 3’-5’
outline the formation of a DNA double helix by hydrogen bonding between nitrogenous bases.
complementary DNA nucleotides form hydrogen bonds between the nitrogenous bases, forming two strands (double) that winds around each other (helix)
state why DNA strands must be separated prior to replication
the two strands of the parent molecule must separate to act as a template for the DNA strands
Describe the movement of DNA polymerase
DNA polymerase moves along the parent DNA strand from the 3’ to the 5’ the complementary daughter strand is built from 4’ to 5’.
describe the action of DNA polymerase iii in pairing nucleotides during DNA replication
It adds the complementary nucleotides
outline the process of transcription, including the role of RNA polymerase and complementary base pairing
transcription is the process of creating mRNA copies from DNA. with RNA polymerase which catalyzes the reaction that synthesizes DNA for replication
define translation
process in which a protein is synthesized from the information delivered through mRNA
outline the role of messenger RNA in translation
the mRNA acts as a template for recruiting and assembling the amino acids to create the desired proteins/peptides
explain how using a 4 letter nucleic “language” can code for a “language” of 20 amino acid letters in proteins
the 4 nucleic bases combine in 3 letter sequences that defines differences amino acids
outline the process of the PCR
multiply DNA samples to allow for testing and experimentation
explain the use of tag DNA polymerase in the PCR
it amplifies pr synthesizes DNA or gene of interest for various downstream applications
use a genetic code table to deduce the mRNA icodon(S) given the name of an amino acid
DNA Seuqunce = TACATTCGATTACCCATC
AUG UAA GCU AAU GGG UAG ->
met-stop-ala-asn-gly-stop
deduce the DNA sequence that produced mRNA=UUAGCGGGCAUA
AAT CGC CCG TAT
