BISC 101 Week 4 Reading

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Last updated 6:22 AM on 5/31/26
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18 Terms

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Primary structure of a protein

-The sequence of amino acids in a polypeptide

-Stabilized by peptide bonds only

-order of R groups affects molecule’s functions

e.g. Hemoglobin, has a valine instead of glumate at the 6th position, causing sickle cell.

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Secondary structure of a protein

-Formation of a helices and B-pleated sheets in a polypeptide

  1. a-helix (alpha-helix), coiled polypeptide backbone.

  2. b-pleated sheet (beta-pleated sheet), 180° bent peptide chain that folds.

-Stabilized by hydrogen bonds

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Tertiary Structure

A protein’s 3D shape

-has five types of interactions that support its structure

  1. Hydrogen bonds

  2. Hydrophobic interactions

  3. Van der Waal interactions: electrical attractions

  4. Covalent bonds

  5. Ionic bonds

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Quarternary Structure

-Combination of subunits

-Individual subunits are held by tertiary level of bonds

  1. Dimers: consists of 2 identical subunits

  2. Tetramers: consists of 4 subunits: 2 identical a units and 2 identical b units.

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Macromolecular machines

groups of proteins that assemble to carry out a function

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Table of protein structures at different levels

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Protein fucntions

Catalysis

Defence

Movement

Signalling

Structure

Transport

Substrates

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Catalysis

-speeds up reactions

-enzymes: proteins that functions as catalyst

-effective at catalysis due to variety of functional groups present in amino acids

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Defence

antibodies

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Movement

-moving the cell or large molecules and other types of cargo inside the cell.

e.g: actin and myosin

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Signalling

carrying and receiving signals from cell to cell

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Structure

Make up body components and form internal skeleton of individual cells

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Transport

Allow molecules to enter ot exit cells

carries molecules throughout body

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Substrates

-reactants in catalyzed reaction

-binds and reacts at an active site

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How enzymes work

-Substrates fit into an enzyme and react (like a key and a lock)

-substrates undergo conformational change so reactants can bind to an active site

-substrates are held in place until transition state is reached

-Lowers activation energy

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Transition state

high-energy, unstable state that molecules must reach for a chemical reaction to occur

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Activation energy

Minimum energy required to proceed a reaction.

Present in all reactions even if its spontaneous

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Free energy

-amt of energy in a system that is usable

-highest during transition state (old bonds broken, new bonds formed)