MACROMOLECULES PROTEINS WHAT ARE PROTEINS Proteins are the
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MACROMOLECULES PROTEINS
WHAT ARE PROTEINS? • Proteins are the most diverse molecules in living organisms. • Make up 50% of most cells EXTREMELY IMPORTANT IN LIVING THINGS! • Involved in almost everything that cells do. • Shape (Structure) is directly related to what they do (Function) STRUCTURE FUNCTION ENZYMES: Special proteins that help reactions happen in cells (more on these later)!
JUST SOME EXAMPLES OF WHY PROTEINS ARE IMPORTANT: • Structural building blocks: – Hair (karatin) – Fingernails (karatin) • Functional Molecules – Antibodies (identify and remove harmful particles from body – Immune System) – Hemoglobin (transports oxygen through body) – Protein Carriers (move substances in and out of cells) • AND SO MUCH MORE!!!!!
FROM DNA TO PROTEIN Each Gene on the DNA codes for a different polypeptide One Gene, One Polypeptide e id pt e pe l ly imp po a s tein A o s I pr is e n e A g ction e a s NA D of
FROM DNA TO PROTEIN The Genetic information in DNA codes SPECIFICALLY for production of PROTEINS and NOTHING ELSE. No Carbs! N Lip o ids !
. WHAT ARE PROTEINS MADE OF? REVIEW: 1) What is a Monomer? The building block of polymers (macromolecules) 2) What is the monomer of a Carbohydrate? A Monosaccharide A protein is a polymer made up of monomers called: 3) What are the monomers of Lipids? Glycerol and Fatty Acids Amino Acids (AAs)
AMINO ACIDS All AAs have: • • A Carboxyl Group (-COOH) An Amino Group (-NH 2) A Hydrogen Atom (-H) A Side Chain (-R) • Also called an R group We are focusing on the AAs in plants and animals. Other types of organisms have different AAs. There are 22 different R groups. Therefore, 22 different Amino Acids Essential Aas (10) • Body cannot make, so you must consume them. • meat, fish, eggs. Non-essential Aas (12) • Body can make. • Nuts, seeds, beans
THE 22 AMINO ACIDS MAIN IDEA: The R groups differ between AAs giving them different chemical properties: There are 2 AAs missing here. They were discovered relatively recently. • Acidic • Basic • Polar • Non-Polar
DNA POLYPEPTIDE Protein Synthesis. The process by which a protein is made is called DNA Contains Genes One gene tells the cell which order to put the AAs in to create a specific protein. The AAs are linked together by Peptide Bonds A chain of Amino Acids is called a Polypeptide.
LEVELS OF PROTEIN STRUCTURE • The different R groups on the AAs attract and repel each other in different ways. • This is why proteins are so varied and can fulfill so many functions. • There are four levels of protein structure, increasing in complexity, depending on how the AAs interact with each other. Primary Structure Amino Acid Sequence of a Polypeptide Secondary Structure Areas of coils and pleated sheets due to hydrogen bonding within a polypeptide Eg. Hair Tertiary Structure Quaternary Structure Overall shape of a polypeptide Eg. Hormones Shape of multiple polypeptides interacting together. Eg. Enzymes
CHANGING THE ORDER OF AAs CHANGES THE PROTEIN • If the structure of a polypeptide is changed, it will effect the function of the resulting protein. STRUCTURE FUNCTION. USING THE CODE, DECIPHER THE SENTENCES "Willfdfd Code fdfdfdfd = it = will = you = do ORIGINAL: 1) 2) 3) ________ _______ ? _______ _______ ? you do it? " "Do you will it? more: http: //www. city-data. com/forum/writing/1115620 -two-sentences-have-same • ad. In this analogy, words represent _______and the sentences represent words-but. html#ixzz 40 Sz 6 Oz 6 s"Will you do it? " __________. "Do you will it? " you change the meaning of the • If you change the order of the ______, __________. The new sentence may have a different meaning or not make sense at all. • Similarly, If the order of ______are changed, the _________ will fold up differently, resulting in a protein with a different ______ and therefore different _______, or a protein that does not work.
SICKLE CELL ANEMIA • Sickle cell anemia is a genetic disorder. • Red blood cells contain an important protein, hemoglobin. • One AA is replaced by another in the polypeptide (glutamate valine) • The change causes the red blood cell to become crescent-shaped (sickled). • Causes clots in vessels resulting in severe fatigue to death.
PROTEIN DENATURATION • When the structure of a protein is changed due to an external stress. • Stresses – – Heat Radiation Change in salt concentration Change in p. H • Stresses cause the protein to uncoil or change shape, changing its function. • Change can be temporary or permanent.
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