(BIOL 101) Module 1: Lesson 5B - Proteins and Nucleic Acids Vocab List

they should put shading tarps around campus

carry out a majority of cell functions (more than 50% of it’s mass); diverse functions ← vary a lot in structure (unique 3d shapes ooo); shape determines function

protein

What are the 8 functions of proteins?

hormonal, receptor, contractile/motor, structural, enzymatic, defensive, storage, transport

function: coordinates an organism’s activities; ex. insulin - secreted into pancreas, takes up glucosre —> regulates bld sugar

hormonal proteins

function: responding to chemical stimuli for cell; built into the membrane of nerve cells detect signaling molecs. from other nerve cells

receptor protein

function: movement; responsible for cilia & flagella undulations; exs. actin & myosin which are responsible for muscle contraction

contractile/motor proteins

function: support; exs. keratin - protiein of hair, horns, feathers, etc., collagen & elastin - provide fibrouse framework in animal connective tissues

structural proteins

function: selectively acceleration chemical reactions; ex. digestive ____ catalyze hydrolysis of bonds in food molecs.

enzymatic proteins

function: protect against disease; ex. antibodies - inactivate & help destroy viruses + bacteria

defensive proteins

function: store amino acids; exs. casein - the milk protein, major source of amino acids for mammal babies, ovalbumin - protein of egg whites, amino acid source for developing embryo

storage proteins

function: transport of substances; exs. hemoglobin - iron-containing protein of vertebrate blood, transports oxygen from lungs to body,,, other proteins that move molecules across cell membranes

transport proteins

facilitate (makes it easier/help them happen) chemical reactions, proteins that act as catalysts

enzymes

chemical agents that speed up chemical reactions without being consumed by the reaction; reusable

catalyst

protein monomers; contain both amino & carboxyl functional groups around a central carbon, also have an ‘R group’; linked together by dehydration reactions to form polypeptides; 20 used for proteins in ALL organisms

amino acids

bonds that hold polypeptides together; formed through dehydration reactions

peptide bond

amino acid polymers; a functional protein consists of 1 or more of these, each folded into a specific shape

polypeptide

side chain within an amino acid; 20 different ones

"R" group

the linked chain of peptide bonds; only first amino acid (N-terminus/engine) has a free amino group; only the last amino acid (C-terminus) has a free carboxyl group —> where new amino acids are always added

backbone of polypeptide

the sequence of amino acids in the polypeptide chain; N term-C term

primary structure

starts to fold due to interactions of atoms in the polypeptide backbone; forms = α-helices & β-sheets

secondary structure

3D shape, folding involving side chains; determined by interactions of the atoms in side chains (R groups); hydrophilic amino acids found on surface of protein, hydrophobic amino acids found inside of protein - side chains interact with both

tertiary structure

multiple polypeptide chains come together to form complex; interactions of multiple, individual polypeptides; not all proteins have these

quaternary structure

proteins that provide a protective environment where proteins can fold spontaneously

chaperonins

the disruption of a protein; can be caused by changes in pH, temp, & salt concentration; not always permanent, proteins can refold if the correct environment’s restored

denature

genetic information/material; polymers of nucleotides; exs. DNA & RNA

nucleic acid

nucleic acid monomers

nucleotide

polymer of nucleic acid; stores hereditary info of a cell

deoxyribonucleic acid (DNA)

Nucleic acids have ____.

Proteins have ____.

phosphodeister bonds; peptide bonds

polymer of nucleic acid; assists in protein production

ribonucleic acid (RNA)