REFLECTION 26: SUMMARY

Hey Biochemians! As we have come to the end of this Biol 1362 course and final exams are right around the corner I thought what better way to end this blog than with a summary to help everyone study. At the end of studying a topic I like to answer all the learning objectives for that topic without using any resources. Then I like to mark it and critique my answer using a fine tooth comb lol. It really helps me so I hope this helps you guys too. Below I have attached all the learning objectives for each topic studied. Happy Studying!

 

TOPIC 1-The Cell (2)

Describe the theory of endosymbiosis

Explain the function of organelles in eukaryotic cells

Describe the relationship between the structure of organelles and their function

Explain the physical constraints on cell size from an evolutionary perspective and describe the adaptations observed in response to these limitations

 

TOPIC 2- Carbohydrates (3)

Identify ketoses and aldoses and tests to distinguish between them.

Draw Fischer and Haworth projection formulae for named tetrose, pentose and hexose sugars.

Define: stereoisomers, diastereoisomers, enantiomers, epimers, anomers and give named

examples.

Distinguish between D & L sugars.

Identify chiral carbons and calculate the number of stereoisomers a molecule can have.

Recognise hemiacetals, hemiketals, acetals and ketals and the significance to reducing and nonreducing sugars.

 Describe the redox reactions of monosaccharides.

Write reactions for glycoside formation, including ring formation.

Identify and draw common disaccharides.

Relate polysaccharide structure to function

Design a flow chart to elucidate the nature of unknown carbohydrates in the laboratory.

 

TOPIC 3- Amino acid & Protein Chemistry (3)

State the different classes into which amino acids may be grouped and give named examples of

amino acids belonging to each class.

Describe the acid-base behavior and ionization of amino acids and define the term ampholyte.

Calculate the pI of any amino acid given its pK values.

Draw and interpret titration curves and utilize the Henderson-Hasselbalch Equation to predict

the ratios of ionized species at given pH values.

Describe the formation and characteristics of peptide bonds.

Describe how pH and ionic strength affect protein solubility.

Define what is meant by protein primary structure and outline the possible outcomes of altering

amino acids within a protein.

Explain what is meant by sequence homology and how it might be used to elucidate functions of

proteins

Describe protein secondary structures and the impacts of proline and glycine on secondary

structure.

Define tertiary and quaternary structures and briefly describe the importance of disulphide

bridges.

Describe the phenomenon of protein denaturation and renaturation.

 

TOPIC 4- Enzymes (4)

Define the terms: apoenzyme, holoenzyme, coenzyme, prosthetic groups, isoenzyme,

metalloenzyme, metal-activated enzyme, active site, transition state, activation energy.

Briefly describe different hypotheses proposed to explain enzyme specificity and catalysis.

List the mechanisms which are used to regulate enzyme activity within living cells.

Briefly describe the six broad groups into which enzymes are classified and give named

examples from each class

Use the Michaelis-Menten and Lineweaver-Burk equations to determine kinetic parameters for

enzymes and relate them to the equation of a hyperbolic curve and a straight line respectively

List the assumptions inherent in the derivation of the Michaelis-Menten equation

Distinguish between different kinds of reversible enzyme inhibitors based on the mode of

binding as well as on the effect of the inhibitor on enzyme KM and Vmax values.

Describe how and why pH and temperature affect enzyme activity

Use enzyme units to define enzyme activity.

 

Topic 5- Glycolysis (3)

 List the types of cells/tissues which must rely on glycolysis to provide energy and explain the

reasons for this dependence

State the other purposes served by this pathway

List the names of enzymes catalyzing each reaction

List the substrates and products of each reaction

Describe the sub-cellular location of the pathway and how the cofactors are regenerated

State the sites where ATP is generated

Describe how the pathway is regulated

Describe what happens in the pathway under aerobic and anaerobic conditions: what products

are formed and what cofactors are limiting

Outline how galactose and fructose enter glycolysis

Outline how glucose released from glycogen enters glycolysis

Outline how arsenate affects glycolysis

 

Topic 6Overview of Metabolism (2)

Show how acetyl-CoA is central to the catabolism of the macronutrients protein, carbohydrates

and lipids.

State how the tricarboxylic acid cycle generates reducing power

Describe how the electron transport chain utilizes reducing power to generate an

electrochemical gradient that is in turn used to generate chemical power in the form of ATP

Describe how 2,4-DNP and rotenone affect the ETC

 

TOPIC 7- Lipids (2)

Define the terms: lipid, amphiphilic (amphipathic) and differentiate between hydrolysable and

non-hydrolysable lipids and between simple and complex lipids.

State the roles of different kinds of lipids.

Use different nomenclature to represent fatty acids.

Relate structures of lipids to their physical properties and reactions.

Relate structures of lipids to their functions.

List the functions of eicosanoids

Identify the different classes of lipids from their chemical formulae

 

TOPIC 8- Nucleotides and Nucleic Acids (2)

Distinguish between nucleosides & nucleotides, between purines & pyrimidines and between

RNA and DNA.

Outline the functions of nucleotides as: building blocks of nucleic acids, sources of energy used

to drive unfavourable reactions and components of coenzymes

Describe the nature of the phosphodiester bridge and how it gives polarity to polynucleotides

and the labile nature of this bond in RNA relative to DNA

Describe the factors which facilitate specific base pairing and state the observations on DNA

composition made by Erwin Chargaff.

Describe the features of the Watson-Crick model of DNA (B-DNA) including the factors which

contribute to the stability of the double helix.

Describe how B-DNA differs from A- and Z-DNA.

Describe the factors which contribute to the flexibility of the DNA molecule

Describe the spontaneous reactions which can take place in DNA: deamination, depurination

and reactions between adjacent thymine bases

Describe the hyperchromic effect and the effect of high salt concentration on the melting

temperature of double-stranded DNA.

Describe the factors which promote the hydrolysis of ATP

References:

Featured Image: http://icandystocks.blogspot.com/2013/03/stock-wise-summary-of-brokerage-views.html

University of the West Indies BIOL 1362 Lecture Topics

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