Zachary Wolff

Sintich AP Biology 2nd Period

November 27, 2015

Biochemistry

Summary and Artifact #1

Standards: 4.A.1: a1-4, b1-3
Proteins have numerous functions. One of those functions is in chemical reactions as
enzymes. Those enzymes are used in the regulation of the metabolism. They act is a catalyst in
this case to speed up the reaction. They do so by lowering the activation energy necessary for the
reaction to occur. Other functions of proteins are Structure (keratin and collagen), Carriers &
transport (hemoglobin), Signaling (hormones and insulin), Receptors & binding (cell surface
receptors), Contractile & motor (actin and myosin), and Defense (antibodies). Protein structure
can be divided into monomers (amino acids) or polymers (polypeptides). Monomers are
constructed of twenty amino acids.those monomers then join into a polymer through a
dehydration reaction which in turn creates peptide bonds. Amino acid structures consist of a
central carbon ( carbon). Attached to the central carbon are the Carboxyl group (-COOH),
Amino group (NH2), Hydrogen atom, and the Side chain (R group). Amino acids can be polar/
charged (hydrophilic), or nonpolar. The building of proteins is done through the process of a
dehydration synthesis reaction of two or more amino acids. Next, the Carboxyl group (-COOH)
and the Amino group (NH2) are joined by a covalent peptide bond (C-N). One end of
polypeptide is free (NH2) = N-terminus. One end of polypeptide is free (-COOH) = C-terminus.
The repeated N-C-C sequence is backbone of polypeptide chain. Function of the protein is
dependent upon the structure of the protein. Four levels of protein structure exist. The first level
is so appropriately named the Primary level. This is where the amino acids are linked together by
peptide bonds. The next level is the Secondary level. Hydrogen bonds are introduced which in
turn create either an alpha or beta fold. The third, or Tertiary level is where all the bonds exist
together and begin to form even more complex bonds ( increased Hydrogen bonds, Disulfide
bridges, Ionic bonds, and Van der Waals interactions). The fourth and final level is the
Quaternary level. This is where the overall protein shape is revealed. Some factors that may
affect protein structure are pH, Salt concentration, and Temperature. If the environment is not
just right a protein will denature (unravel, lose confirmation, become dysfunctional).
Chaperonins are simply protein molecules that assist with the proper folding of other proteins.

PROTEINS

ARTIFACT

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