Proteins
List 5 examples of the function of proteins in our bodies.
1. Alph-keratin forms hair and fingernails 2. Hemoglobin carries oxygen in blood throughout the body. 3. Enzymes in saliva, stomach, and small intestine help digest food. 4. Actin and myosin, muscle proteins enable all muscle movement. 5. Anti-bodies help fight disease.
Two proteins and describe how their structure relates to their function.
1. Antibodies: Its Y shape makes it easier to capture the foreign molecule. 2. Collagen: forms cartilage and tendons and gains its strength from its 3 stranded rope-like structure
Four Levels of Protein Structure:
1. Primary 2. Secondary 3. Tertiary 4. Quaternary
How many standard protein building blocks are there?
20
Proteins usually contain___ to _____amino acids hooked end to end in many combinations.
50 to 2,000
Describe how cystic fibrosis occurs.
A protein called CFTR folds incorrectly.
What is the monomer of proteins?
Amino acids
What is sickle cell anemia caused by?
An error in just one amino acide, specifically in an incorrect position.
Defensive proteins:
Antibodies in the immune system
Secondary Structure:
Coil or fold of the parts of the peptide chain.
Peptide bond:
Covalent link between amino acids
Protein catalyst:
Enzyme
Where do we find alpha-keratin on our bodies?
Fingernails and hair
Structural protein:
Hair, tendon, ligament fibers
Transport proteins:
Hemoglobin
Siginal proteins:
Hormones
What protein causes fireflies to light up?
Luciferase
Contractile proteins:
Muscles
Storage proteins:
Ovalbumin (protein in egg whites)
Protein:
Polymer constructed from amino acide monomers.
Describe the process of how proteins are made.
Proteins are created through the procersses of transcription, translation and protein folding. During transcription, genes are transcribed intno complementary strands of messenger RNA (mRNA). Then translation begins and ribosomes make proteins by using the mRNA instructions and the genetic code to join amino acids together in ther firhg order. Three adjacent mRNA nucleotides (a triplet) encode one amino acid. To finish folding most proteins require the help of chaperone proteins.
Quaternary Structure:
Proteins that have two or more polypeptide chains.
Tertiary Structure:
Refers to the overall 3 dimensional shape of a polypeptide.
Please describe the "protein folding problem" and explain why it is important for scientists to understand this problem.
The protein folding problem is that scientists cannot crack the code that governs folding of a protein even though they can determine a proteins amino acid sequence. Since diseases like Alzheimer's, cystic fibrosis and mad cow are thought to result from misfolded proteins, knowlege of how their structure is determined could improve treatment of those diseases.
Primary Structure:
The unique sequence of amino acids
R group:
The variable part of the amino acid
What medical use does the venom of cobras, scorpions and puffer fish serve?
These venoms contain small proteins that act as nerve toxins and have been made into a drug called Prialt which is used to treat severe pain that is unresponsive to morphine.
Why do ships in the northwest Pacific Ocean leave a green trail?
This lighted eerie green trail is produced by a protein in jellyfish that is produced when the jellyfish are jostled by the ships.
Denaturation
When polypeptide chains unravel their shape.
Where else is it found?
feathers, wool, claws, scales, horns and hooves.
Where a protein chain curves into a corkscrew, that section is called _______. Where it forms a flattened strip, it is a _______ _________
helix beta sheet
Spider webs ands silk fibers are made of _________. Scientists would like to use this fiber for _________ or _________
strong pliable protein fibroins bullet proof vests or artificial joints