Proteins are sequences of amino acids joined by peptidic bonds. These sequences determine their function in cells. They characterize for expressing primary, secondary, tertiary, and quaternary structure.
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Amino acids are organic molecules. They are composed of a central carbon, one hydrogen atom, one carboxyl group, one amine group, and one R group. The composition of the R group is what makes them different from each other.
Proteins are amino acid polymers linearly arranged and connected by peptidic bonds. These molecules characterize by their different structures.
- The primary structure refers to the sequence in which the amino acids are arranged in the chain.
- The secondary structure is the folding that the polypeptide chain adopts through the hydrogen bonds between the atoms.
The hydrogen bonds are set between the -CO- and -NH- groups of the peptide bond (the first as an H acceptor and the second as an H donor). These conformations with less free energy, and therefore, more stable. The most common secondary structures are alpha-helix and beta-sheet.
Many proteins can express both secondary structures, alpha-helix, and beta-sheet.
- Proteins acquire a tertiary structure that makes them more stable. Lineal polypeptides get folded and turn into a shape that makes them more stable in the environment and capable of accomplishing their biological role. The hydrophilic R-groups stick in the center of the polypeptide, facing the protein interior, and avoiding interaction with water.
- When proteins are composed of more than one polypeptide subunit, they arrange in a fourth structure, named quaternary structure.
The many functions that proteins accomplish depend on the aminoacids sequences.
So, the appropriate locations in this concept map are as follow,
a) amino acids
b) functions
c) peptide bonds
d) central carbon
e) primary structure
f) secondary structure
g) R-group
h) tertiary structure
i) quaternary structure
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