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Orca Share Media1536282065056
Orca Share Media1536282065056
Protein!
Proteins
• Primary structure
– A.K.A. “the sequence”
• Secondary structure
– Short stretches form distinct ‘substructures’
• Helices
• Strands
• Turns & Loops
• Tertiary structure
– The arrangement of secondary structure elements with
respect to each other
Primary structure
For example:
-Lys-Val-Phe-Ala-Met-Cys-Leu-Leu-Arg-Val-COO-
• Secondary structure
– Short stretches form distinct ‘substructures’
• Helices
• Strands
• Turns & Loops
• Tertiary structure
– The arrangement of secondary structure elements with
respect to each other
Secondary structure - helix
Secondary structure - strands
Secondary structure - turn
Proteins
• Primary structure
– A.K.A. “the sequence”
• Secondary structure
– Short stretches form distinct ‘substructures’
• Helices
• Strands
• Turns & Loops
• Tertiary structure
– The arrangement of secondary structure elements with respect to
each other
From sequence to structure?
“When you understand the amino acids, you
understand everything”
The amino acids
A short introduction
One amino acid
Hydrophobic
Aliphatic Ala, Leu, Ile, Val
Aromatic Phe, Tyr, Trp, (His)
Hydrophilic
Polar Asn, Gln
Alcoholic Ser, Thr, (Tyr)
Charged Arg, Lys, Asp, Glu, (His)
Inbetween:
Sulfur-containing Met, Cys
Special Gly (no R), Pro (cyclic)
•Hydrophobicity
•Size
•Charge
•Secondary structure preference
•Alcoholicity
•Aromaticity
•And on top of that there are some special characteristics like bridge forming
by cysteines, rigidity of prolines, titrating at physiological pH of histidine,
flexibility of glycines, etc.
Hydrophobic
Aromatic
Hydrophilic - neutral
Hydrophilic - charged
Sulfur - containing
Really special
Cysteines are extra special
Key points about the character of amino acid
side chains
• Certain residues do this hydrophobic packing better than others, and those
residues are thus good for a helix.
Remember: AMELK
Secondary structure - strands
Secondary structure - strands
• Also strands pack because hydrophobic packing of side chains along the length of
the strand.
• Certain residues do this hydrophobic packing better than others, and those
residues are thus good for a strands. b-branched residues (Ile, Thr, Val) are very
good for strands, and so are the large hydrophobic residues.
•
Remember: VITWYF
Secondary structure - turn
Secondary structure - turns
• To create a turn the backbone needs to be bent pretty sharply, and some residues
are really good at that.
• Glycine is special because it is so flexible, so it can easily make the sharp turns and
bends needed in a b-turn. Proline is special because it is so rigid; you could say
that it is pre-bent for the turn. Aspartic acid, asparagine, and serine have in
common that they have short side chains that can form hydrogen bonds with the
own backbone. These hydrogen bonds compensate the energy loss caused by
bending the chain into a
• Remember: PSDNG
A common theme
• Most secondary structure elements are
located at the surface of the protein
Actually, it is all done by water. Water does not like hydrophobic surfaces. When a
protein folds, exposed hydrophobic side chains get buried, and release water of its sad
duty to sit against the hydrophobic surfaces of these side chains.
Water is very happy in bulk water because there it has on average 3.6 H-bonds and
about six degrees of freedom.
So, whenever we discuss protein structure, folding, and stability, it is all the entropy of
water, and that is called the hydrophobic effect.
When hydrophobic
objects come together in
water, the number of
unhappy waters go
down, and that is good
for stability.