Bio 1201 5

•Macromolecules

large polymers

•Polymer

long molecule consisting of many similar building blocks

Monomers

repeating units that serve as building blocks

•Enzymes

specialized macromolecules that speed up chemical reactions (catalysts)

•Dehydration reaction

when two monomers bond together through the loss of a water molecule

•Hydrolysis

a reaction that uses water to disassemble monomers

Carbohydrates

macromolecules made of sugars

•Monosaccharides

molecular formulas that are usually multiples of CH2O (mono means 1, so a single sugar component)

Disaccharide

Two monosaccharides

Glycosidiclinkage

the covalent bond between two monosaccharides

•Polysaccharides

polymers of sugar

•Starch

a storage polysaccharide of plants consisting of glucose molecules, with an alpha 1-4 glycoside linkage

•Glycogen

storage polysaccharide in animals consisting of glucose molecules, with an alpha 1-4 glycoside linkage

•Cellulose

component of cell walls in plants consisting of glucose molecules attached by a beta 1-4 glycosidic linkage

•Chitin

a structural polysaccharide found in the exoskeleton of arthropods

•Lipids

hydrophobic molecules such as fats, phospholipids, steroids, etc.

•Fats

glycerol + fatty acids

•Fatty acid

a carboxyl group attached to a long carbon skeleton

Triacylglycerol (triglyceride)

in a fat, three fatty acids joined to glycerol by an ester linkage

Saturated Fatty acids

maximum number of hydrogens (NO DOUBLE BONDS)

•Unsaturated fatty acids

have one or more double bonds

Trans fats

when the double bond does NOT alter the overall structure (no changes in the tail)

•Phospholipid

two fatty acids and a phosphate group attached to glycerol

Steroids

lipids characterized by a carbon skeleton consisting of four fused rings

•Cholesterol

a steroid, a component in animal cell membranes, the precursor which other steroids are synthesized.

•Polypeptides

are unbranched polymers built from amino acids

•Protein

biologically functional molecule that consists of one or more polypeptides.

•Amino acids

organic molecules with amino and carboxyl groups

•Peptide bonds

the link between amino acids in a polypeptide.

Primary structure

sequence of amino acids

Secondary structure

the structure that results from hydrogen bonds between the polypeptide backbone. Can form either a coil called α helix and a folded structure called a β pleated sheet

•Tertiary Structure

the overall all shape of a single polypeptide strand, resulting from interactions of the R groups (ie the functional groups attached to the amino acids)

•Hydrophobic interactions

interaction of hydrophobic compounds

•Disulfide bridges

two sulfurs interaction

•Quaternary structure

when two or more polypeptide chains form one macromolecule

•Denaturation

the loss of a proteins native structure

•X-ray crystallography

a method for determining protein secondary, tertiary, and quaternary structure involving an x-ray beam.

•Gene

unit of inheritance consisting of DNA

•Nucleic acid

AGCT, DNA called nucleotides.

•Deoxyribonucleic acid (DNA)

made with deoxyribose

•Ribonucleic acid (RNA)

made with ribose

•Gene Expression

synthesis of mRNA then protein synthesis ( transcription + translation)

•Polynucleotides

multiple nucleotides

•Pyrimidines (cytosine, thymine, and uracil)

have a single six-membered ring

•Purines (adenine and guanine)

have a six-membered ring fused to a five-membered ring

•Double Helix

two polynucleotides spiraling around an imaginary axis forming DNA

•Antiparallel

when two strands if DNA run in opposite directions

Bioinformatics

using computer software to find patterns in data

•Genomics

the study of whole genomes of different species

•Proteomics

the study of large sets of proteins including their sequence.