Flashcards
Biochemistry_Unit 1 part 1
Cards in this deck (111)
- 1Hydrolysis ReactionH2O + AB --> AH+ + BOH-
- 2Condensation Reaction/Dehydration ReactionBOH- + AH+ --> AB + H2O
- 3Oxidation Reaction- Loses electrons
- Loses Hydrogen
- Gains Oxygen - 4Reduction Reaction- Gains electrons
- Gains Hydrogen
- Loses Oxygen - 5What functional group is this? R-O-HHydroxyl
- 6What functional group is this? O || R --C--OHCarboxyl
- 7What functional group is this? H | R - N | HAmino
- 8What functional group is this? O || R - O - P - OH | OHPhosphate
- 9What functional group is this? O || R - C - HAldehyde (Carbonyl)
- 10What functional group is this? O || R - C - R"Ketone (Carbonyl)
- 11What functional group is this? R - S - HSulfhydryl
- 12What is a radioisotope?- Nuclei of an element is unstable so it decays
- Gives off particles of matter that can be detected as radioactivity
- Then turns into an unstable radioactive isotope - 13Hydrophobic- Does not like water
- Is Non - Polar
- Is not attracted to water - 14Hydrophilic- Likes water
- Is Polar
- It is attracted to water - 15What are Peptide bonds?Protein bonds, long chains of amino acids
- 16Protein structure?Primary Structure
- It's about the overall
3-D shape of protein, and it's range of bonding interactions between amino acid R groups - 17Protein structure?Secondary Structure
- it's about the interactions between atoms in the backbone
- 18Protein structure?- Tertiary Structure
- it's dependent on the amino acid side chains
- 19Protein Structure?Quaternary Structure
- Hydrogen bonds, polar and non-polar attractions, and disulphide linkages help hod together the multiple polypeptide
- 20Essential or Non-Essential Amino Acid? HISTIDINEEssential Amino Acid
- 21Essential or Non-Essential Amino Acid? ISOLEUCINEEssential Amino Acid
- 22Essential or Non-Essential Amino Acid? LEUCINEEssential Amino Acid
- 23Essential or Non-Essential Amino Acid? LYSINEEssential Amino Acid
- 24Essential or Non-Essential Amino Acid? METHIONINEEssential Amino Acid
- 25Essential or Non-Essential Amino Acid? PHENYLALANINEEssential Amino Acid
- 26Essential or Non-Essential Amino Acid? THREONINEEssential Amino Acid
- 27Essential or Non-Essential Amino Acid? TRYPTOPHANEssential Amino Acid
- 28Essential or Non-Essential Amino Acid? VALINEEssential Amino Acid
- 29Essential or Non-Essential Amino Acid? ALANINENon-essential Amino Acid
- 30Essential or Non-Essential Amino Acid? ARGININENon- Essential Amino Acid
- 31Essential or Non-Essential Amino Acid? ASPARAGINENon- essential Amino Acid
- 32Essential or Non-Essential Amino Acid? ASPARTIC ACID (ASPARTATE)Non-essential Amino Acid
- 33Essential or Non-Essential Amino Acid? CYSTEINE (CYSTINE)Non- essential Amino Acid
*Our body can break it down to make it essential - 34Essential or Non-Essential Amino Acid? TYROSINENon- essential Amino Acid
* Our body can break it down to make it essential - 35Essential or Non-Essential Amino Acid? GLUTAMIC ACID (GLUTAMATE)Non- essential Amino Acids
- 36Essential or Non-Essential Amino Acid? GLUTAMINENon-essential Amino Acid
- 37Essential or Non-Essential Amino Acid? GLYCINENon- essential Amino Acid
- 38Essential or Non-Essential Amino Acid? PROLINENon- essential Amino Acid
- 39Essential or Non-Essential Amino Acid? SERINENon- essential Amino Acid
- 40Starch is what form of carbohydrates?Polysaccharide
- 41Glycogen is what form of carbohydrates?Polysaccharide
- 42Cellulose is what form of carbohydrates?Polysaccharide
- 43Chitin is what form of carbohydrates?Polysaccharide
- 44Does starch consist only of glucose? True/FalseTrue, starch consists only of glucose
- 45Is Glycogen stored only in animals? True/FalseTrue
- 46Glycogen does not consist of glucose. True/FalseFalse
- 47Humans can digest Cellulose. True/FalseFalse
- 48Chitin is a component of what in nature?It is a component of exoskeleton of insects, spiders, and crustaceans
- 49How does Chitin's molecule look like?Looks like cellulose but with an N group
- 50What is Glycosidic Linkage?- Covalent bond formed between two monosaccharides
- The oxygen leftover from the water, creates the linkage between the two
monosaccharides - 51What molecule is this, and structure?Glucose Molecule, Monosaccharide
- 52What molecule is this, and structure?Fructose Molecule, Monosaccharide
- 53What molecule is this, and structure?Galactose Molecule, Monosaccharide
- 54Glucose + Fructose --> ?Sucrose + H2O
- 55Glucose + Galactose -> ?Lactose + H2O
- 56Glucose + Glucose -> ?Maltose + H2O
- 57What types of Fats are there?- Triglycerides
- Phospholipids
- Steroids
- Waxes - 58Saturated and Unsaturated Fatty Acids, are what component of Fat?Triglycerides
- 59Unsaturated Fatty Acids are unhealthy. T/FFalse
- 60A Healthy Fat has double bonds in it's molecule. T/FTrue
- 61Unsaturated Fats have kinks. T/FTrue, Unsaturated Fats are healthy fats
- 62Unsaturated Fats have double bonded kinks, which makes them have less hydrogens, and therefore more healthy. T/FTrue
- 63Saturated Fatty Acids contain straight chains (no kinks) T/FTrue
- 64Saturated Fats are unhealthy/healthy, and why?They are unhealthy because they contain straight bonds, and come from Animal Fats
- 65Triglycerides are formed from what type of reactions?Condensation Reactions
- 66What do phospholipids contain?- 1 glycerol molecule, 2 fatty acid chains, 1 phosphate group (PO4)
- 67Phospholipids have what types of heads?Phospholipids have a
polar head (hydrophilic) (i.e. is the phosphate in centre molecule)
Non-polar head (hydrophobic) (i.e. hydrocarbon, the ends of carbon) - 68Steroids consist of what?- consist of 4 fused carbon rings
- 69Steroids function as what?Steroids function as messengers across cell membranes
- 703 types of Steroids in the body?- Hormones: physiological responses
- Bile Salts: helps to emulsify fats
- Cholesterol: converted into bile salts and vitamin D - 71Waxes consist of what?Waxes consist of fatty acid chains which are linked to carbon rings or alcohols
- 72What are waxes used for?They're used for waterproofing. Birds and Plants naturally contain them, so that way they can be protected from the rain.
- 73Nucleic Acids function to do what?They function to direct growth and develop of every living thing through it's chemical code (RNA and DNA)
- 74What is the coding for DNA?Adenine (A) <-> Thymine (T)
Guanine (G) <-> Cytosine (C) - 75What is the coding for RNA?Adenine (A) <-> Uracil (U)
Guanine <-> Cytosine (C)
*ignore Thymine (T) - 76RNA structure for nucleotidesThere is an oxygen with the hydrogen in the sugar (pentane shape)
- 77DNA structure for nucleotidesDNA structure has a missing oxygen with the hydrogen in the sugar (Pentane) shape group
DE-OXY-RIBO-SUGAR
- 78What is DNA's function?Allows transmission of hereditary intro from parent to offspring (aka. child)
- 79What is RNA's function?- Involved in protein synthesis and regulating gene expression
- Also genomes of most viruses - 80Nitrogen bases play what role in DNA and RNA?- Contain 4 different bases in DNA and RNA
(i.e. DNA: A <-> T and G <-> C) or
(i.e. RNA: A <-> U and G <-> C) - 81What's the relationship between Nucleotides and Nucleic Acids?Nucleic Acids are POLYMERS of Nucleotide MONOMERS
- 82What are enzymes?They are catalytic proteins, and help lower the activation energy, that's needed to get a reaction started
**Note: they do NOT add on to the reaction, and their names end with "-ase" - 83How do enzymes contribute to someone with a fever?- The heat speeds up a reaction, but the high temperature can kill proteins and cells
- So enzymes are needed to lessen the heat, but allow the reaction to occur - 84How do enzymes work in a reaction?-Enzymes bind to it's substrate(S)
- While enzymes and substrate are joined, the catalytic action of the enzymes converts the substrate to the products of the reaction
- 85What particular reactions do enzymes use when catalyzing?Either the:
- Lock and Key model
or
- Induced Fit Model - 86How does the Lock and Key Model work?- The shape of the substrate molecule is exactly complementary to the shape of the active site
- 87How does the Induced Fit Model work?- approach of the substrate causes a change in the shape of the active site
- The active site becomes fully complementary to the substrate molecule only after the substrate is bound
*Hint: handshake; is forced to conform to the other hand's shape
- 88What is the Allosteric Site?- an effector molecule binds to the enzyme molecule, at a location other than the active site (aka. other than the activation energy site)
- 89What's an effector molecule?It's binds to a specific enzyme/protein, and then controls it biological activity
- 90What happens when an activator binds to an allosteric site?- It stabilizes the shape that has a functional active site
- 91What happens when an allosteric inhibitor binds?It stabilized the inactive form of the enzyme
- 92How would an reaction look like without the enzyme?
- 93What are some factors that affect enzymes?- Temperature
- pH
- Cofactors (no presence)
- Enzyme Inhibitors - 94How does the Temperature affect Enzymes?- Up to a certain lime the sped of enzymatic reaction increases along with the temperature
- Beyond an optimal temperature the speed of enzymatic reaction drops sharply
- Human enzyme optimal temp is 35-40 Celcius - 95How does the pH affect Enzymes?- Optimal pH values for most enzymes is pH 6-8
- Pepsin (stomach enzyme) is an exception, it works at a pH of 2 - 96What are cofactors?- Substance (other than substrate) whose presence is essential for enzyme activity
- Can be inorganic (i.e. metal atoms, zinc, iron, copper, etc.)
- If organic, it's called coenzyme (i.e. vitamins) - 97What are Enzyme Inhibitors?Certain chemicals selectively inhibit the action of specific enzymes
- 98What are some types of inhibitors?- Competitive Inhibitors
- Non - Competitive Inhibitors - 99How do Competitive Inhibitors affect Enzymes?Reduce productivity of enzymes by blocking substrates from emerging from active sites
*Hint: The competitive inhibitor is competing against the substrate for the chair in musical chairs, by inhibitor sitting on the chair it prevents the substrate from emerging - 100How do Non - Competitive Inhibitors affect Enzymes?They impede enzymatic reactions by binding to another part of the enzyme. This causes enzymes to change shape and for active site to become unreceptive to substrate.
(ie. antibiotics inhibit specific enzymes in bacteria) - 101What is Allosteric Activation?The active site becomes available to the substrates when a controlled molecule binds to a different site on the enzyme, so that it operates properly
- 102Allosteric deactivationThe active site becomes unavailable to the substrates when a controlled molecule binds to a different site on the enzyme
- 103What does exocytosis mean?- Expels molecules out of the cell
- 104What happens in Exocytosis?- Vesicles are budded off from Golgi Tendon
- Which fuses with the plasma membrane, and opens up
- Which then opens up it's contents to the extracellular fluid (outside of cell)
- 105What is a Hypotonic Solution?-Concentration of solute is higher inside the cell rather than outside the cell
- Water wants to dilute, will go into cell
- 106What is a Isotonic Solution?Concentration of solution = to outside of solution
- 107What is a Hypertonic Solution?Concentration inside of cell is less than outside; solute leaves the cell
- 108Is Diffusion passive or active transport?Passive Transport,
Molecules go from High concentration
to a Low concentration, requires NO energy (NO ATP) - 109Is Facilitated Diffusion passive or active transport?Passive Transport, requires no energy
- 110Is Osmosis passive or active transport?Passive Transport
- 111Ion Pump is it active or passive transport?Active, goes from low concentration to high concentration
Information
- Description
- High School Diploma Biology Flashcards on Biochemistry_Unit 1 part 1, created by anam.saeed98 on 06/03/2016.
- Created by
- anam.saeed98
- Views
- 1
- Rating