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Samenvatting

Summary Medical Biochemistry Notes

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Answered learning objectives that cover core topics from biochemistry that are relevant to medical students

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Geüpload op
15 mei 2025
Aantal pagina's
32
Geschreven in
2023/2024
Type
Samenvatting

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Learning Objectives (Building Blocks).........................................................................................1
Self-Generated Questions..................................................................................................7
Learning Objectives (Membrane Structure and Lipids)............................................................13
Self-Generated Questions.........................................................................................................17
Learning Objectives (Organization of the Cell).........................................................................17
Self Generated Questions.........................................................................................................21
Learning Objectives (Protein Structure and Function).............................................................21
Learning Objectives (Cytoskeleton)..........................................................................................27


Learning Objectives (Building Blocks)
1. Compare and Contrast the catabolic and anabolic processes in biochemistry with special
emphasis on the energy molecules generated and used in these processes.

Compare Contrast
Anabolism • Anabolic processes are responsible
for building up tissues and organs,
which result in the growth and
differentiation of cells
• Has three requirements
1. Energy (ATP)
2. Reducing Power
3. Carbon skeleton
•Result in the transfer of reducing
equivalents → NAD+/NADH and Uses reducing agents to build
NADP+/NADPH (NADPH/NADH)

• Are closely linked to nutrition
Catabolism which can lead to anabolic • Breakdown of complex molecules
processes (after absorption → build- into several smaller molecules.
up of tissues and organs); digestion • Exergonic
→ catabolic processes • Energy released (ATP) → can be
used to synthesize complex
• The CAC is an amphibolic molecules
pathway.
Produces reducing agents (NADH2,
FADH2)

, 2. Name the key pathways in metabolism and describe their start and endpoints.
Inputs Outputs Catabolic, Anabolic,
Amphibolic

Glycolysis Glucose, NAD+, 2 ATP Pyruvate, NADH, 4 ATP Catabolic

TCA Cycle Acetyl-coA, NAD+, NADH, FADH2, CO2, Amphibolic
FADH2 GTP

Oxidative FADH2, NADH, ADP H2O, ATP Catabolic
Phosphorylation +Pi, O2

Glycogenesis 1 ATP + Glucose Glycogen Anabolic
or
Glucose-6-Phosphate

Glycogenolysis Glycogen Glucose-6-Phosphate Catabolic

Hexose Monophosphate G6P NADPH, Ribose-6- Amphibolic
Shunt (PPP) Phosphate

Fatty Acid Synthesis Acetyl-CoA Fatty acid, TAGs Anabolic

Fatty Acid Degradation Fatty Acid, Acyl-CoA Catabolic


Amino Acid Catabolism Pyruvate: A, C, G, S, T, Glucose Catabolic
W
Oxaloacetate: N, D
Fumarate: D, Y, F
Succinyl-CoA: I, M, V
Alpha-ketoglutarate: R, E,
Q, H, P
Acetyl-CoA: I, L,W
Acetoacetyl-CoA: L, K, F,
W, Y

Urea Cycle Ammonia (NH3), CO2, urea, fumarate
Aspartate, ATP

Purine and Pyrimidine Pyrimidine Nucleotides Beta amino acids, Catabolic
Catabolism Ammonia

Purine Catabolism Purine Nucleotides

Purine and Pyrimidine
Synthesis

, 3. Identify the key molecules that are the branch points for various biochemical pathways involved
in energy production.

● Glucose-6-Phosphate → Glycogenesis, PPP, and Glycolysis
● Acetyl-CoA → TCA, ketone bodies, FA synthesis
● Glycerol-3-phosphate

4. Identify the major biomacromolecules’ function, composition, key structural and chemical
features, and their monomeric subunits.
Biomolecule Function Composition Structural Feature Chemical Feature
Nucleotides ● Nucleotides are responsible for ● Composed: ● RNA has -OH ● G-C has a
building DNA and RNA - Ribose sugars on the 2’ carbon triple
● DNA is responsible for (RNA) and in the ribose hydrogen
encoding genomic information deoxyribose sugar sugar
bond →
responsible for cellular (DNA) ● DNA has -H on
functions - Phosphates the 2’ carbon in strong
● RNA has several forms and - Purine (Guanine the deoxyribose ● A-T ha a
can be both single and double and Adenine) or sugar double
stranded Pyrimidine ● DNA and RNA hydrogen
○ mRNA → translated (Cytosine, are linked bond →
into protein (has a Thymine, Uracil) together via
bases phosphodiester slightly
transient structure) weaker
● A purine always bonds
○ tRNA → helps with ● The hydroge
pairs with a ● DNA is double
the making a protein pyrimidine stranded and bonds are
(has a discrete antiparallel between the
structure) ● Synthesized and hydrogen and
○ rRNA → ribosomal read in the 5’ nitrogen in
the purine
RNA has a discrete →3’ direction
+pyrimidine
structure ● phosphate
○ siRNA → responsible groups are
for post- negatively
transcriptional charged
regulation making RNA
and DNA
○ microRNA → negatively
process and charged
regulatory




Protein • Diet • Composed of Amino ● Most amino ● Contains
● Source of energy Acids (A.A) acids are chiral carboxyl
● Source of amino acids to build • Are polymers of (A. As) ● Most group
through peptide bonds biologically ● Contain and

, new protein. • Read in the N → C relevant amino amide
• Catalysis terminus acids are L ● Contain and
• Structure amino acids R group
• Receptor signalling ● Linked ● folding is
• Carriers of small molecules together via determined
• Movement peptide bonds by
• Communication hydrophobic
• Transport interactions
Carbohydrates • Polysaccharides + ● Ribose = 5 ● Contain
• Responsible for: Disaccharides = linked carbon sugars hydroxyl
- Energy (ATP) together by glycosidic ● Hexoses = 6 groups
- Energy Storage (glycogen, bonds (glycosidic bonds = carbon sugars ● Can be
starches [amylose, ether bonds) ● Di/polysaccs aldose or
amylopectin], cellulose) • Composed of sugar linked together ketoses
- Immune regulation monomers by glycosidic ● Hydrophilic
- Physical barrier • Don’t have particular (ether) linkages
- Regulation of folding polarity ● Carbohydrates
- Structural proteins • Sucrose = glucose + for glycolipids
- blood antigens fructose alpha (1→2) beta and
• Maltose = glucose + glycoproteins
through either
glucose alpha (1→4) bond formation
• Lactose = glucose + ● Glycogen =
galactose beta (1→4) highly
• Glycogen, starches, and branched
cellulose are all polymers
glucose chain
of glucose
alpha (1→4) and
alpha (1→6)
glycosidic
linkages
● Starches
- Amylose alpha
(1 → 4)
- Amylopectin
alpha (1→4) and
alpha (1→6);
highly
branched
● Cellulose beta
(1→4)
Lipids • Storage • Made by ester bonds ● No inherent ● Hydrophobic
• Energy (more energy that between glycerol and fatty directionality (?) (or
carbohydrates through metabolism) acids ● Linked via amphiphilic)
• Compartmentalization • bigger polar heard and ester bonds ● amphipathic
small tail = micelles (has both
equal size polar head and polar and
nonpolar tail = cell nonpolar
membrane portion)
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