| A | B |
|---|
| immunoglobins | antibodies, immunesystem |
| transport | movement of materials, hemoglobin for oxygen |
| regulatory | hormones, control of metabolism |
| structural | coverings and support, skin, tendons, hair, nails, bone |
| movement | muscles, cilla, flagella |
| all proteins are composed of what? | amino acids |
| how many common amino acids are there?what type are they? what form are they? | 20, alpha, L |
| what is the exception to all amino acids being L? | glycine |
| what is attached to a alpha carbon? | a primary amine |
| zwitterion | how well an acid and base are based on pH and the type of amino acid |
| carboyhydrates are what form? | the D form |
| hydrophobic | water fearing, non polar side chain |
| hydrophilic | water loving, polar, neutral chains both charges |
| what amino acid has mild sedative properties? | tryptothan |
| what amino acid is linked to the inability to process | phenylalanine |
| all amino acids starting with S or T are | polar, neutral amino acids |
| All amino acids beginning with P,I or M are? | neutral non-polar side chains |
| polar amino acids | like water |
| Leu-Gly-Ala-Val | neutral, nonpolar |
| Asn-Cys-Gln | neutral, polar |
| Asp-Glu | acidic, polar side chains (negative) |
| Arg-Lys-His | Basic, polar side chains (positive) |
| proteins are polymers made up of.. | amino acids |
| peptide bond | how amino acids are linked together to make a protein |
| Primary structure | the order of amino acid residues in a protein (or polypeptide) |
| peptide bonds are between which two elements? | carbon and NH |
| After forming a peptide bond what remains? | amino acid residue |
| The end with the free amine is the? | N-terminal residue |
| An amino acid with an end habing a free acid | C-terminal |
| N-terminal residue is written on what side? | the left |
| stick model | pretty confusing more meaningful with smaller molecules |
| space filling | idea as to shape and presence of pores or holes |
| ribbon | shows different types of secondary structure |
| Cartoon | a structural view but quick to draw |
| secondary structure of proteins | a result of hydrogen bonding between two amino acids with the same protein |
| in secondary structures of proteins, long chains curl or fold into what kinds of structures? | a regular repeating one |
| the two common secondary structures are: | alpha helix and beta pleated sheet |
| secondary structure adds what properties to a protein? | strength and flexibility |
| what does an alpha helix depict | how amino acids are linked to produce the helix |
| in an alpha helix carboxyl groups always point... | in the same direction |
| protofibril | when multiple strands entwine |
| in beta pleated sheets, carbonyl groups point in what direction? | opposite |
| silk fibroin | the main protein of silk has a beta sheet |
| B pleated sheets are mostly composed of | glycine and alanine |
| collagen is a family of..they make up what amount of proteins in humans? | related proteins, 1/3 |
| what does collagen provide strength to? | bones, tendons, skin, and blood vessels |
| tropocollagen | forms triple helix |
| what is the major use of vitamin C? | to convert proline and lysine residues to 4 and 5 hydroxy, which residues can then form crosslinks |
| scurvy | disease from lack of vitamin c results in skin lesions, bleeding gums and fragile blood vessels |
| tertiary structure of proteins includes | fibrous and globular proteins |
| fibrous proteins, soluble? formed from? types? | insoluble in water, form from connective tissues, and are silk, collagen and Beta Keratins |
| globular proteins soluble? formed? 3-d? | soluble in water, form by cell proteins, and have a tertiary structure |
| tertiary structures result from? | side chains, which help maintain specific structure |
| possible side chain reactions in tertiary structures: (4) | similar solubilities, ionic attractions, attraction between sidechains, and covalent bonding |
| oxidation of cystine | crosslink formation |
| hydrophobic attractions (tertiary) | attractions between R groups of non-polar amino acids |
| hydrogen bonding (tertiary) | interaction between polar amino acids R groups |
| ionic bonding (tertiary) | attraction of charged amino acid R groups |
| are most proteins single peptide strands ? | no |
| quaternary structure of prteins are: | combinations of several proteins |
| conjugated protein | incorporate another type of group that performs a specific function |
| prosthetic group | non amino acid components |
| hemoglobin | oxygen transport protein of red blood cells |
| myoglobin | oxygen storage protein of skeletal muscles |
| hemoglobins and myoglobins rely on what group as the binding site for oxygen? | the heme group |
| in the lungs there is an abundance of O2 so oxygen is picked up by what? | hemoglobin |
| hemoglobin does what when blood reaches the cells | they give up O2 |
| fetus takes oxygen from a mother by diffusion across what? | the placenta |
| what type of hemoglobin does the fetus have that is more efficent?when does the production of it stop? | fetal hemoglobin, just before birth |
| sickle cell hemoglobin is caused by what? | changing one amino acid in each beta protein component |
| denatured | a disorganized protein that no longer acts as intended |
| coagulate | clumping |
| if you add heat to a denatured protein, what then happens? | it is a coagulated protein |
| hydrolysis of a protein results in what? | a protein being reduced to simpler peptides and amino acids |
| change in pH does what to proteins? | alters their solubility and changes their shape |
| where are the following protein hormones? gastrin, glucagon, insulin, prolactin, and vasopressin | stomach, pancreas,pancreas, pituitary, pituitary |
| somatropin and other hormones are now produced by.... | engineered bacteria |
| Immunoglobin | a y shaped protein made up of 4 protein chains linked by disulfide bonds |
| x | x |
| x | x |
