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Molecules, Biodiversity, Food and Health

Molecules, Biodiversity, Food and Health

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Published by George Noorland

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Published by: George Noorland on May 24, 2011
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05/24/2011

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Emily Summers
1
AS Unit F212:
 
Molecules, biodiversity, food and health
Module 1 - Biological moleculesBiological molecules
D
escribe how hydrogen bonding occurs between water molecules, and relate this and other properties of water to the roles of water in living organisms.
 
D
escribe, with the aid of diagrams, the structure of an amino acid.
Structure of an Amino AcidStructure of Glycine
All
amino acids have the samegenera
l
structure, a carboxy
l
group,an amino group attached to a carbonatom (-NH
2
) but the R group isvariab
l
e, and that is the on
l
ydifference between amino acids.
 
Emily Summers
2
D
escribe, with the aid of diagrams, the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides andpolypeptides.Explain, with the aid of diagrams, the term
 primary structure
.
Explain, with the aid of diagrams, the term
secondary structure
 with reference to hydrogen bonding. Explain, with the aid of diagrams, the term
tertiary structure
, withreference to hydrophobic and hydrophilic interactions, disulphidebonds and ionic interactions
Ionic Interactions
weak attractionsbetween oppositely charged parts themolecule
D
isulfide Bonds
Two molecules of anamino acid close together, the sulphur atoms in them bond together forming thisbond. (E.g. Cysteine)
C
ondensation reactions makepeptide bonds between amino acids.
A
mo
l
ecu
l
e of water is re
l
eased.Its reversib
l
e, and by adding a watermo
l
ecu
l
e you can break the peptidebonds. This is ca
ll
ed hydro
l
ysis.
 
Emily Summers
3
Hydrophobic
Water repelling groups near together in a protein they clump.Hydrophilic
Water attracting groups are likely to be pushed outside, affecting theprotein¶s final structure.
Explain, with the aid of diagrams, the term
q
uaternary 
 
structure
, with referenceto the structure of haemoglobin.
The quaternary structure tends to be determined bythe tertiary, when it involves multiple polypeptides.E.g. Haemoglobin has a quaternary structure, it has4 polypeptide chains.
D
escribe, with the aid of diagrams, the structure of a collagen molecule
Collagen is a strong protein that is fibrous. It is asupportive tissue in animals; it is made of threepolypeptide chains that are very tightly coiled into atriple helix, interlinked by covalent bonds. Mineralsare able to bind to this helix to increase rigidity.
y
Tendons are made up mostly of collagen
y
Walls of arteries contain collagen to preventbursting from high pressure blood in them
y
Cosmetic treatment for lips for a fuller appearance
Compare the structure and function of haemoglobin (as an example of a globular protein) and collagen (as an example of a fibrousprotein).
H
aemoglobin Collagen
G
lobular protein Fibrous ProteinLarge variety of amino acids in it¶s primarystructure35% of primary structure is glycineHas a prosthetic group- haem
D
oesn¶t contain a prosthetic groupMostly wound into alpha helix structures Mostly left handed helix structures
D
escribe, with the aid of diagrams, the molecular structure of alpha-glucose as an example of a monosaccharide carbohydrate.
 
Monosaccharide carbohydrate, a hexosesugar because it has six carbon atoms inevery molecule. The structure determines itssolubility so it can be easily transported. It¶sa source of energy for animals and plants.Its chemical bonds have lots of energy inthem.

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