Backlinks
1 Proteins
All cell uses rybozome to force KBhBIO101AminoAcids together to make proteins. And yes, if you have a high energy source that would not require ATP from itself (make life from not life), you could get proteans to fold.
1.1 Protean Shapes
Proteins, when unfolded, is a long chain of amino acids. When they are folded in different configurations, you get a working protean.
The functions of proteins are varied because the primary sequence can be varied, effectively building any shape protein to do its specific function
Form = function is the idea that the shape or form a protein takes through the combination of primary, secondary, tertiary, or quaternary structure determines how it will then function. Any changes to the structure will have some impact on its function and the more the structure is affected the more the function is likely to impacted.
Functions => defense, movement, structure, transport, cell to cell signaling, etc.
"The Protean Folding Problem" => can we find the fold of the protean just by the unfolded amino acids?
1.1.1 Protean primary structure
The linear order of amino acids — staring from the amino terminus (N, exposes the Amine end) and moving to carbonxy terminusi (C, exposes the Carboxy terminus).
Average protean is about 300 amino acids long.
1.1.2 Protean secondary structure
Folding a protean without concern to the amino acid side chains. The folding is only concerned with being stabilized with dipole attraction to hydrogen.
Two main secondary structures: the alpha helix and beta sheet.
Figure 1: Screen Shot 2020-09-21 at 3.15.49 PM.png
*No ionic attractions between backbone because after the dehydration reaction (polymerization), the positive and negative of the two ends of the backbone of the amino acid is combined to cancel out the charge*
Proline (p) is a little weird: Side chain bonded with the H2N+ as well as the carbon => "the helix breaker": most likely cause a bend instead of a structured area due to its unusual circular bonding.
1.1.3 Protein Tertiary Structure
Bonds in the 3D Structures
- Non-polar sidechains: Vandervaull's Forces (a.k.a LDF)
- Ionic sidechains: what bonds do you think?
- Disulfide bonds: cysteine animo acids will bond their sulfur together
- Polar sidechains: hydrogen bonds
All of these bonds, together, makes the 3D geometry of the protean.
Proteins fold in order of attraction strength.
- Proteas "whiggle" — brounian motion
- This is also a part of the difficulty in folding protean
1.1.4 Protein Quaternary Structure
Exists only for certain proteins which independently locks together.
Hemoglobin does this! It contains multiple sets of side chains that needs folding once again.
1.2 Shooting images of proteins
- NMR spectroscopy
- X-rays
#flo #disorganized
1.3 Enzymes
A specific type of proteins that's… kinda fun! KBhBIO101Enzymes