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Proteins: Folded Polypeptides
Proteins: Folded Polypeptides
Proteins: Folded Polypeptides
FOLDED POLYPEPTIDES
PRIMARY STRUCTURE
The sequence of amino acids
MIL1 sequence:
>gi|7662506|ref|NP_056182.1| MIL1 protein [Homo sapiens]
MEDCLAHLGEKVSQELKEPLHKALQMLLSQPVTYQAFRECTLETTVHASGWNKILVPLVLLRQMLL
ELTRLGQEPLSALLQFGVTYLEDYSAEYIIQQGGWGTVFSLESEEEEYPGITAEDSNDIYILPSDN
SGQVSPPESPTVTTSWQSESLPVSLSASQSWHTESLPVSLGPESWQQIAMDPEEVKSLDSNGAGEK
SENNSSNSDIVHVEKEEVPEGMEEAAVASVVLPARELQEALPEAPAPLLPHITATSLLGTREPDTE
VITVEKSSPATSLFVELDEEEVKAATTEPTEVEEVVPALEPTETLLSEKEINAREESLVEELSPAS
EKKPVPPSEGKSRLSPAGEMKPMPLSEGKSILLFGGAAAVAILAVAIGVALALRKK
length: 386amino acids
Anne-Marie Ternes
PRIMARY STRUCTURE
Infinite variety
The number of possible sequences is
infinite
An average protein has 300 amino acids,
At each position there could be one of 20
different amino acids
= 10390 possible combinations
Most are useless
Natural selection picks out the best
SECONDARY STRUCTURE
The folding of the N-CC backbone of the
polypeptide chain
using weak hydrogen
bonds
SECONDARY STRUCTURE
Dr Gary Kaiser
TERTIARY STRUCTURE
The folding of the polypeptide into
domains whose chemical properties are
determined by the amino acids in the
chain
MIL1 protein
TERTIARY STRUCTURE
QUATERNARY STRUCTURE
Some proteins are
made of several
polypeptide subunits
(e.g. haemoglobin has
four)
Protein Kinase C
Max Planck Institute for Molecular Genetics
Text 2007 Paul Billiet ODWS
QUATERNARY STRUCTURE
These subunits fit together to form the
functional protein
Therefore, the sequence of the amino
acids in the primary structure will influence
the protein's structure at two, three or
more levels
Result
Protein structure depends upon the
amino acid sequence
This, in turn, depends upon the sequence
of bases in the gene
PROTEIN FUNCTIONS
Protein structure determines protein
function
Denaturation or inhibition which may
change protein structure will change its
function
Coenzymes and cofactors in general may
enhance the protein's structure
Fibrous proteins
Involved in structure: tendons ligaments
blood clots
(e.g. collagen and keratin)
Contractile proteins in movement: muscle,
microtubules
(cytoskelton, mitotic spindle, cilia, flagella)
Globular proteins
most proteins which move around (e.g.
albumen, casein in milk)
Proteins with binding sites:
enzymes, haemoglobin, immunoglobulins,
membrane receptor sites
CATALYTIC: enzymes
STORAGE: ovalbumen (in eggs), casein (in milk), zein
(in maize)
TRANSPORT: haemoglobin
COMMUNICATION: hormones (eg insulin) and
neurotransmitters
CONTRACTILE: actin, myosin, dynein (in microtubules)
PROTECTIVE: Immunoglobulin, fibrinogen, blood
clotting factors
TOXINS: snake venom
STRUCTURAL: cell membrane proteins, keratin (hair),
collagen