Proteins and Amino Acids

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1

Amino Acid

Hydrophilic. Many of them create a polypeptide. two create a dipeptide. Amino acid is the building block of protein. Structure: Has an amine on the left (NH2) and a carboxyl (COOH with a double bond to one O) on the right. In the middle is a Carbon attached to the N and C and also is attached to a hydrogen and an R. R is a variable. In proteins it can be 20 different things which means there are 20 different types of amino acids.

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Amino acids with hydrophobic, partially charged, and fully charged R groups.

R group is....
Hydrophobic: Nothing in R group has an electronegative charge.
Partially charged (polar): One or more of the atoms have an electronegative charge. hydrophilic
Fully Charged: One of the atoms are ionic and have 1 extra or less electron. Hydrophilic
(im not sure about this card so edit it if you know)

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How To get amino acids

Eat foods with protein (meat dairy nuts etc.) Needed to build protein (muscle hair nails) and can be used as fuel. Your body makes 12 out of the 20 the other 8 are "essential" and must be eaten.

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Proline

Important because it can give a protein a 3D shape. R group is C3 H6 and the N in the anime loses a Hydrogen.

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Cysteine

R group is CH2 with the C connected to a sulfur which connects to a hydrogen. Important because it causes folding in disulfide bonding.

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Dipeptide/polypeptide

Two or more amino acids will bond through dehydration synthesis. Anime will connect to carboxyl. Carboxyl loses its CO and the anime loses one H, dehydration synthesis. A long polypeptide can become a protein by folding and having a purpose.

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Protein

A certain shape of a polypeptide that has a function. Through folding they get a shape. Proteins are in hair muscle and nails.

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Primary Structure

Order of the amino acids.

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Secondary structure

Shape before folding. Has a wag to it.

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Tertiary structure

Shape after the folding.

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Quaternary structure

The tertiary effects between two or more polypeptides inside protein.

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Disulfide bond

Cysteins have sulfur. Sulfurs bond together. fold up the polypeptide.

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Salt bridge

Positively charged r groups attach to negatively charged r groups.

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Zinc Finger

Cofactor: Something that becomes part of the protein structure that is not actually part of the polypeptide. A zinc+ (cofactor) connects two negative r groups. Other + cofactors can also do this.

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Hydrophobic effect

R groups without a charge clump out of contact with polar solvent. In solvent of water hydrophilic amino acids are on the outside and hydrophobic are on the inside.

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Phosphorylation/Dephosphorylation

Can change the tertiary structure after it is created. A triphosphate (ATP) goes by and gives a phosphate to an r group. Dehydration synthesis. ATP becomes diphosphate (ADP) Opposite for Dephosphorylation Not sure if thats exactly right.