Quiz
Wk 10- Introduction to Biochemistry and Clinical Biochemistry
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1What are the “building blocks” for protein macromolecules?
- AAmino acids
- BPolysaccharides
2What are the “building blocks” for polysaccharides?
- Amonosaccharides
- Bglucose
3What are the “building blocks” for nucleic acids?
- Anucleotides
- Bglucose
4A nucleotide consists of three things:
- A nitrogenous base, which can be either adenine, guanine, cytosine, or thymine (in the case of RNA, thymine is replaced by uracil).
- A five-carbon sugar, called deoxyribose because it is lacking an oxygen group on one of its carbons.
- One or more phosphate groups.- ARichtig
- BFalsch
5What are the “building blocks” for lipid aggregates?
- AFatty acids and glycerol
- BFatty acids and omega 3
6What macromolecule/s can be made up of branched chains?
- APolysaccharides
- BMonosaccharides
7How many standard amino acids are there?
- A20
- B6
8How do the standard amino acids differ from one another?
- ASide (R) groups
- BProteins
9Amino acids can be classified according to their R group. Why might it be useful to use this classification? (Hint, might some amino acids with similar R groups have similar properties?)
- AR group differentiates amino group. L and D stereoisomers determine chiralty
- BR group differentiates lipid group. L and R stereoisomers determine chiralty
10What does it mean if something is Chiral?
- AThe property of having a 'left' and 'right' form of a molecule/compound. They cannot be superimposed on each other as they are not 'identical'
- BThe property of having completely identical forms of a molecule/compound. They can be superimposed on each other as they are 'identical'
11Enantiomers are chiral molecules that are mirror images of one another. Furthermore, the molecules are non-superimposable on one another. This means that the molecules cannot be placed on top of one another and give the same molecule. Chiral molecules with one or more stereocenters can be enantiomers.
- ARichtig
- BFalsch
12What does the L and D in amino acids stand for?
- AThe L in front of an amino acid is a shortened scientific notation for “levorotatory', the D means 'dextrorotatory'. The terms dextrorotatory and levorotatory refer to an optical property that can be observed and measured in a laboratory, by shining a beam of polarized light through a medium containing the substance.
- BThe L in front of an amino acid is a shortened scientific notation for “levorous', the D means 'dextrous'. The terms dextrous and levorous refer to an optical property that can be observed and measured in a laboratory, by shining a beam of polarized light through a medium containing the substance.
13Levorotatory is (of a compound) having the property of rotating the plane of a polarized light ray to the left, i.e. anticlockwise facing the oncoming radiation.
- ARichtig
- BFalsch
14Levorotatory is (of a compound) having the property of rotating the plane of a polarized light ray to the right, i.e. anticlockwise facing the oncoming radiation.
- ARichtig
- BFalsch
15Dextrorotatory (of a compound) is having the property of rotating the plane of a polarized light ray to the right, i.e. clockwise facing the oncoming radiation.
- ARichtig
- BFalsch
16What is a peptide bond?
- Aless than 50 amino acids in the linear sequence
- Bmore than 50 amino acids in the linear sequence
17Explain why amino acids are important.
- AAmino acids are a source of energy, they contribute about 10-15% of metabolic energy and are precursors to other important biomolecules
- BAlthough Amino acids are not a source of energy, they contribute about 5-10% of cattabolic energy and occasionally are precursors to other important biomolecules
18Select Three examples of important Disaccharides.
- ASucrose
- BLactose
- CMaltose
- DFructose
19How is Diabetes mellitus diagnosed?
- ABlood glucose test
- BGlycosuria test
20Select the Four major roles of Protein.
- APlays a role in immunity, growth, regulation of genes and communication (hormones, cells)
- BGenerates movement in cells and tissues (e.g. myosin in muscle) and structural support
- CBreaks down covalent bonds and transforms one chemical into another (e.g. enzymes)
- DCarries and stores small molecules or ions (e.g. haemoglobin carrying oxygen)
- EPrevents urine incontinence, hair growth and eye function
21Give an example of important Monosaccharides
- AD-Glucose, D-Fructose, D-Ribose
- BD-Glucose, D-Fructose, D-Lactose
22Select three (3) major functions of lipids.
- AStorage - fuels, insulation, protection, heat production
- BStructural - biological membranes
- CSpecific biological actions - Biological messengers - intracellular and extracellular, Co-factors for enzymes, Electron carriers and effectors
- DStorage - ATP, Warmth, Oxytocin
23Select Four examples of lipid aggregates.
- Amicelles
- Bliposomes
- Cmembranes
- Dlipoproteins
- Elysosomes
24Select four (4) of the major functions of carbohydrates in a cell
- A– structure
- B– nucleic acids (DNA and RNA)
- C– cell to cell communication
- D- energy source
- E- makes up the cytoplasm
25What is Beer ’s Law?
- Aa more concentrated solution absorbs more light than a more dilute solution does.
- Ba more diluted solution absorbs more light than a more concentrated solution does.
26What is Lambert’s Law?
- Astates that absorbance of a material sample is directly proportional to its thickness
- Bstates that absorbance of a material sample is irregardless of its thickness
27What is the combined Lambert-Beer Law?
- AAs the light passes through a solution, the intensity of light transmitted decrease, exponentially with increasing path length (lamberts law) and with increasing concentration of the absorbing substance (Beers law)
- BAs the light passes through a solution, the intensity of light transmitted decrease, exponentially with increasing path length (lamberts law) and with decreasing concentration of the absorbing substance (Beers law)
28Lipids may not be considered true macromolecules because of their structure. Briefly explain.
- ABecause individual monomers (fatty acids) are not covalently bound to each other in a macromolecular structure
- Bindividual monomers (fatty acids) are not ionic compounds to each other in a macromolecular structure
29Can two sugar molecules have different configurations despite having the same molecular formula?
- AYes - because of stereoisomers
- BNo - because there is no such thing
30Is it more convenient to use Absorbance or Transmittance to determine the concentration of a substance?
- ATransmittance - The difference between the intensity of the incident light beam Io and the intensity of the light transmitted by the solution It
- BAbsorbance - The difference between the intensity of the incident light beam Io and the intensity of the light transmitted by the solution It
31What is the general structure of an amino acid
- Aalpha (α) carbon, carboxyl group, amino group, ‘R’ group
- Balpha (α) hydrogen, carboxyl group, amino group, ‘R’ group
32Explain the term Diabetes mellitus
- Ahigh blood sugar levels over a prolonged period.
- Blow blood sugar levels over a prolonged period.
33Spectrophotometers can be used to measure the absorbance of light of a particular wavelength by a certain material. What is meant by the term absorbance?
- AThe amount of light absorbed by the material used depending on thickness
- BThe amount of light unabsorbed by the material used depending on thickness
34Why is the selection of optimal analytical wavelength important for spectrophotometric measurement?
- ABecause different compounds absorb light at different wavelengths, a spectrophotometer can be used to distinguish compounds by analyzing the pattern of wavelengths absorbed by a given sample.
- BBecause some compounds do not absorb light at different wavelengths, therefore a spectrophotometer can not be used to distinguish compounds by analyzing the pattern of wavelengths absorbed by a given sample.
35List two examples of terms that describe different secondary structures that can be found in proteins.
- AFinal folded form of the protein.
- Bα-helix, β-sheet and Turns
36What is meant by the term 'Protein Primary Structure'
- ALinear sequence of amino acids.
- BFolds, Helices and Strands
37What is meant by the term 'Protein Secondary Structure'
- ASecondary protein structure is the general 3-dimensional form of local segments of a protein. The most common secondary structures are alpha helices and beta-pleated sheets.
- BThis process happens in the nucleus. In the cytoplasm, ribosomes will interact with the transcript and create a protein (polypeptide) from individual amino acids.
38What is meant by the term 'Protein Tertiary Structure'
- AThe general 3-dimensional form of local segments of a protein. The most common structures are alpha helices and beta-pleated sheets.
- BTertiary structures involve packaging and folding the secondary structures into compact globular regions called protein domains.
39What is meant by the term 'Protein Quaternary Structure'
- AProtein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex.
- BAmino acids form structures such as alpha helices, beta sheets, and random coils, which in turn fold on themselves
40A peptide bond is a chemical bond formed between two amino acids
- ARichtig
- BFalsch
41Stereoisomers are isomeric molecules that have the same molecular formula and sequence of bonded atoms (constitution), but differ in the three-dimensional orientations of their atoms in space.
- ARichtig
- BFalsch
42A codon is the sequence of 3 consecutive nucleotides on a DNA or RNA strand. It either codes for a specific amino acid in a polypeptide or terminates the polypeptide chain
- ARichtig
- BFalsch
43peptide = less than 50 amino acids in the linear sequence
polypeptide or protein = more than 50 amino acids in the linear sequence- ARichtig
- BFalsch
44Protein Structure
[blank_start]Primary structure[blank_end]
Linear sequence of amino acids.
[blank_start]Secondary structure[blank_end]
Backbone of the polypeptide chain folds into regular geometric structures.
• α-helix
• β-sheet
• Turns
[blank_start]Tertiary structure[blank_end]
Final folded form of the protein.
The native form of the protein.
[blank_start]Quaternary structure[blank_end]
Association of two, or more, polypeptide tertiary structures.
e.g.haemoglobin is comprised of two alpha and two beta polypeptide chains- APrimary structure
- BQuaternary structure
- CTertiary structure
- DSecondary structure
45Lipids are composed of relatively simpler smaller molecules and they can form very large structures through non covalent associations
- ARichtig
- BFalsch
46Unsaturated lipids have a double bond
- ARichtig
- BFalsch
47When lipids are placed in an aqueous solvent, they cluster together forming microscopic lipid aggregates. In a lipid aggregate, the hydrophobic component of lipids are in contact with each other, while the polar head groups are in contact with the aqueous solvent.
- ARichtig
- BFalsch
48Carbohydrate– ‘hydrate of carbon ’ Cn H2nOn (where n ≥3)
- ARichtig
- BFalsch
49Oligosaccharides:
- 2 to 20 monosaccharides
-polysaccharides - ≥20 monosaccharides- ARichtig
- BFalsch
50Carbohydrate - structure
• General name
– according to number of carbons eg. trioses, tetroses,
pentoses, hexoses, heptoses
– according to type: aldose or ketose
• Aldoses
– aldehyde group in the structure
• Ketoses
– ketone group in the structure- ARichtig
- BFalsch
Informationen
- Beschreibung
- Wk 10- Introduction to Biochemistry and Clinical Biochemistry
- Autor
- Jessica Bulley
- Sprache
- English
- Aufrufe
- 35
- Schlagwörter
- Bewertung
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