The Cell Lecture 8

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  • Created by: saraht83
  • Created on: 01-05-16 17:09
Covalent bonds
atoms share one or more pairs of electrons, outer shells full
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Polar covalent bonds
electrons drawn to one nucleus more than other
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Ionic bonds
one atom so electronegative it removes electron from other atom
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Isomers
molecules with same chemical formula, atoms arranged differently
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Structural isomers
differ in how their atoms are joined together
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Optical isomers
carbon atom has 4 different atoms/groups of atoms attached
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Hormonal and regulatory proteins
control physiological processes
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Receptor proteins
receive and respond to molecular signals
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Storage proteins
store amino acids
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Structural proteins
provide physical stability and movement
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Transport proteins
carry substances within the organism
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Genetic regulatory proteins
regulate when, how, and to what extent a gene is expressed
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Proteins
polymers of 20 different amino acids
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Polypeptide chain
single, unbranched, chain of amino acids folded into specific three-dimensional shapes
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Amino acids
carboxyl and amino groups - both acid + base, exist as D-amino acids and L-amino acids
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Methionine
initiates chains of amino acids
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Proline
causes kinks in chains of amino acids
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Cysteine
links amino acid chains together, -SH group reacts with another, forming -**- bond, disulfide bridge
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Amino acids
bond covalently through condensation reaction by peptide linkages
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Primary structure
amino acid sequence
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Secondary structure
alpha-helix right handed coil, hydrogen between N-H and C=O groups on neighbouring amino acids, beta-pleated sheet, two or more polypeptide chains aligned, hydrogen bonds form between chains
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Tertiary structure
macromolecule with specific 3D shape, determined by interactions of R-groups, disulfide bridges, hydrogen bonds, aggregation of hydrophobic side chains, van der Waals forces, ionic bonds
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Protein is heated
secondary and tertiary structures denatured
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Quaternary structure
interaction of subunits by hydrophobic interactions, van der Waals forces, ionic bonds and hydrogen bond
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Conditions affecting secondary + tertiary structure
high temperature, pH changes, high concentrations of polar molecules, non-polar substances
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Energy
the capacity to do work, or the capacity for change
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Potential energy
stored energy
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Kinetic energy
the energy of movement
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Metabolism
sum total of all chemical reactions in an organism
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Anabolic reactions
complex molecules are made from simple molecules
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Catabolic reactions
complex molecules broken down to simpler ones
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First law of thermodynamics
energy is neither created nor destroyed
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Second law of thermodynamics
energy converted from one form to another, some of that energy becomes unavailable to do work
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Entropy
measure of disorder in a system, unless energy is applied to a system, it will be randomly arranged/disordered
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Change in free energy (delta G)
difference in free energy of the product and the reactants
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Delta G is negative
free energy is released
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Delta G is positive
free energy is consumes
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Delta H
total energy added or released
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Delta S
change in entropy, large changes make delta G more negative
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Exergonic reactions
release free energy, catabolism, complexity (order) decreases
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Endergonic reactions
consume free energy, anabolism, complexity (order) increases
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Delta G = 0
forward + reverse reactions balanced
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Delta G values near zero
readily reversible reactions
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Enzymes
lower energy barrier by bringing reactants together
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Enzyme-substrate complex
held by hydrogen bonds, electrical attraction, or covalent bonds
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Enzyme mechanisms
orientation of substrate molecule, physical strain of the substrate molecule, chemical change of substrate molecule
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Induced fit
enzymes change shape when they bind to substrate
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Lysozyme
enzyme found in egg white, saliva + tears, acts as antibiotic, catalyses cutting of polysaccharide chains in bacterial cell walls, catalyses a hydrolysis rection that is spontaneous but not instantaneous
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Feedback inhibition (end-product)
final product non-competitive inhibitor of first enzyme, shuts down the pathway
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Ribozymes
made from RNA, act as biological catalysts
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Other cards in this set

Card 2

Front

electrons drawn to one nucleus more than other

Back

Polar covalent bonds

Card 3

Front

one atom so electronegative it removes electron from other atom

Back

Preview of the back of card 3

Card 4

Front

molecules with same chemical formula, atoms arranged differently

Back

Preview of the back of card 4

Card 5

Front

differ in how their atoms are joined together

Back

Preview of the back of card 5
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