its function is involved in almost everything

(a)  

NH2

(a)  

COO2

(a)  

variable group

(a)  

different for each amino acid

(a)  

confers unique chemical properties to each amino acid like 20 different letters of an alphabet, can make many words (proteins)

(a)  

monomer

(a)  

polymer

(a)  

amino acids

(a)  

polypeptide

(a)  

can be one or more polypeptide chains folded & bonded together

(a)  

large & complex molecules, complex 3-D shape

(a)  

20 different amino acids

(a)  

Forms disulfide bridges

(a)  

covalent cross links betweens sulfhydryls, stabilizes 3-D structure

(a)  

Made up of chains of amino acids

(a)  

Classified by number of amino acids in a chain

(a)  

Fewer than 50 amino acids

(a)  

2 amino acids

(a)  

3 amino acids

(a)  

More than 10 amino acids

(a)  

More than 50 amino acids

(a)  

Typically 100 to 10,000 amino acids linked together

(a)  

Chains are synthesizes based on?

(a)  

Amino acids are composed of?

(a)  

Form when the acid group (COOH) of one amino acid joins with the amine group (NH2) of a second amino acid.

(a)  

Formed through condensation

(a)  

Broken through hydrolysis

(a)  

Directions of polypeptide chain

(a)  

N-terminus

(a)  

C-terminus

(a)  

NH2 end

(a)  

COOH end

(a)  

Polypeptide backbone and can only grow in one direction

(a)  

Primary (1°) structure: Enzyme in tears & mucus that kills bacteria

(a)  

Primary (1°) structure: Amino acid sequence determined by?

(a)  

Secondary (2°) structure: Folding along short sections of polypeptide

interactions, between adjacent amino acids, and forms sections of 3-D structure

(a)  

Secondary (2°) structure: Weak bonds between R groups

(a)  

Secondary (2°) structure: Sections of 3-D structure

(a)  

Tertiary (3°) structure: Interactions between distant amino acids

(a)  

Tertiary (3°) structure: Cytoplasm is water-based and nonpolar amino acids cluster away from water

(a)  

Quaternary (4°) structure: Polypeptide become functional protein

(a)  

Must be consumed in the diet

(a)  

Can be synthesized in the body

(a)  

Cannot be synthesized due to illness or lack of necessary precursors

(a)  

Four levels of structure of the protein

(a)  

Alteration of the protein’s shape and thus functions through the use of:

(a)  

Alteration of the protein’s shape and thus functions through the use of heat, acids, bases, salts, mechanical agitation

(a)  

Primary structure is unchanged by this

(a)  

Provide shelter for folding polypeptides

(a)  

Keeps the new protein segregated from cytoplasmic influences

(a)  

Guide protein folding

(a)  

Protein structure visualized by...

(a)  

Consists of a central carbon with a carboxyl group, a hydrogen, a nitrogen-containing amine group, and a unique side chain

(a)  

no. of side chains

(a)  

no. of unique amino acids

(a)  

no. of essential amino acids

(a)  

no. of nonessential amino acids

(a)  

Amino acids link together with peptide bonds by?

(a)  

Amino acids break apart by?

(a)  

It cause the proteins to fold into precise three-dimensional shapes

(a)  

Determines its function

(a)  

Unfolding a protein

(a)  

Conditions that disrupt H bonds, ionic bonds, disulfide bridges

(a)  

Alter 2° & 3° structure

(a)  

Some proteins can return to their functional shape after denaturation, many cannot

(a)