Biochemistry Quiz 1 + r groups

Glycine

Group A - Nonpolar Amino Acids (Hydrophobic)

Alanine

Group A - Nonpolar Amino Acids (Hydrophobic)

Valine

Group A - Nonpolar Amino Acids (Hydrophobic)

Leucine

Group A - Nonpolar Amino Acids (Hydrophobic)

Isoleucine

Group A - Nonpolar Amino Acids (Hydrophobic)

Methionine

Group A - Nonpolar Amino Acids (Hydrophobic)

Phenylalanine

Group A - Nonpolar Amino Acids (Hydrophobic)

Tryptophan

Group A - Nonpolar Amino Acids (Hydrophobic)

Proline

Group A - Nonpolar Amino Acids (Hydrophobic)

Serine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Threonine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Cysteine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Tyrosine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Asparagine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Glutamine

Group B - Polar Uncharged Amino Acids (Hydrophillic)

Aspartate

Group C - Polar charged Amino Acids (Hydrophillic) (Acidic)

Glutamate

Group C - Polar charged Amino Acids (Hydrophillic) (Acidic)

Lysine

Group C - Polar charged Amino Acids (Hydrophillic) (Basic)

Arginine

Group C - Polar charged Amino Acids (Hydrophillic) (Basic)

Histidine

Group C - Polar charged Amino Acids (Hydrophillic) (Basic)

the most abundant elements in carbon based organisms

C, H, O, N, P, S

hydrocarbons

organic molecules consisting of only carbon and hydrogen

undergo reactions that release a large amount of energy

isomers

compounds with the same molecular formula but different structures and properties

structural isomers

have different covalent arrangements of their atoms

cis-trans isomers

have the same covalent bonds but differ in spatial arrangements

enantiomers

isomers that are mirror images

functional groups

components of organic molecules most commonly involved in chemical reactions

the seven functional groups

• hydroxyl group (O-H)

• carbonyl group (C-O)

• carboxyl group(C-O-OH)

• amino group (H-N-H)

• sulfhydryl group (SH)

• phosphate group (P-O-O-O)

• methyl group (C-H-H-H)

adenine triphosphate

primary energy transferring molecule in the cell

adenosine attached to 3 phosphate group

macromolecules

large molecules composed of thousands of covalently connected atoms

polymer

a long molecule consisting of many similar building blocks

monomers

small building-block molecules

dehydration reaction

occurs when 2 monomers bond together through the loss of a water molecule

builds polymers

hydrolysis

a reaction that is essentially the reverse of a dehydration reaction

disassembles polymers

carbohydrates

sugars and the polymers of sugars

polysaccharides

macromolecules of carbohydrates

storage and structural roles

structure and function are determined by its sugar monomers and the positions of glycosidic linkages

monosaccharides

single sugars

usually have molecular formulas that are multiples of CH₂O

how are monosaccharides classified

• location of carbonyl group

• number of carbons in the skeleton

what are sugars drawn as in aqueous solutions

rings

in non aqueous they are usually drawn linear

disaccharide

a dehydration reaction joins 2 monosaccharides

glycosidic linkage

the covalent bond between monosaccharides

starch

a storage polysaccharide of plants, consists entirely of glucose monomers

the simplest form of starch is amylose

stored mainly in granules within chloroplasts and other plastids

alpha glycosodic linkages

glycogen

a storage polysaccharide in animals

stored mainly in liver and muscle cells

cellulose

a structural polysaccharide comprising plant cell walls

beta glycosidic linkages

• enzymes that digest starch cant hydrolyze beta linkages in cellulose

polymers with alpha glucose are what?

helical

polymers with beta glucose are what?

straight

allows h atoms on one strand to bond with oh groups on another strand

chitin

structural polysaccharide

found in the exoskeleton of arthropods

cells walls of many fungi

lipids

large biological molecule that does not form polymers

little or no affinity for water

consist mostly of hydrocarbons which form nonpolar covalent bonds

function of fats

energy storage

biologically important lipids

fats, phospholipids, and steroids

fats are made of what?

glycerol and fatty acids

glycerol

a three carbon alcohol with a hydroxyl group

fatty acid

carboxyl group attached to a long carbon skeleton

ester linkage

the bond between the fatty acids and glycerol in a fatty acid

triglyceride

3 fatty acids bonded to a glycerol

saturated fatty acids

have the maximum number of hydrogen atoms possible and no double bonds

solid at room temp

most animal fats are saturated

unsaturated fatty acids

have one or more double bonds

liquid at room temp

plant fats and fish fats are usually unsaturated

phospholipids

two hydrophobic fatty acids and a hydrophilic phosphate group are attached to glycerol

lipid bilayer structure in cell membranes

steroids

lipids characterized by a carbon skeleton consisting of 4 fused rings

common in animal cell membranes, regulates membrane fluidity

cholesterol is a steroid component in animal cells

protein functions

structural support, storage, transport, cellular communications, movement, and defense against foreign substances

enzymes

biological catalysts

8 common functions of proteins

• enzymatic proteins

• defensive proteins

• transport proteins

• storage proteins

• hormonal proteins

• receptor proteins

• contractile and motor proteins

• structure proteins

polypeptides

unbranched polymers built from the same set of 20 amino acids

protein

consists of one or more polypeptides

amino acids

monomer of polypeptides

organic molecules with carboxyl and amino groups

r groups differ in amino acids

how are amino acids linked

peptide bonds

carboxyl end (c-terminus) and amino end (n terminus)

primary structure

sequence of amino acids

secondary structure

consist of coils and folds of polypeptide chain due to hydrogen bonds

alpha helix and beta pleated sheet

tertiary structure

determined by interactions between R groups

can be hydrogen bonds, ionic, hydrophobic interactions, van der waals interactions, or strong covalent bonds called disulfide bridges

quaternary structure

results when 2 or more polypeptide chains form one macromolecule

collagen and hemoglobin

denaturation

loss of protein’s native structure

chaperonins

Protein molecules that assist the proper folding of other proteins

nucleotides

monomers of nucleic acids

nitrogenous base, sugar, and phosphate group

nucleoside

sugar and nitrogenous base

phosphodiester bond

the bond that nucleotides build

sugar phosphate backbone - OH group on 3’ carbon of one nucleotide and the next phosphate on the 5’ carbon

double helix

two polynucleotides spiraling

antiparallel

backbones run in opposite directions

purine

2 carbon rings

adenine and guanine

pyrimidines

one carbon ring

cytosine, uracil, thymine

complementary pairing

purines will pair with pyrimidines

A to T

C to G