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APBIO: CH.5 structure and function of macromolecules

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Alexander Ravajy

on 6 September 2010

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Transcript of APBIO: CH.5 structure and function of macromolecules

SWBAT state the structure and function of macromolecules What are the 4 important biological molecules related to life? State their respective function and structure What are the 4 levels of structural conformation proteins must undergo before becoming active? What impacts to heat and pH have on protein structure? Most macromolecules are polymers, built from monomers Polymer: long chain molecules made of repeating subunits called monomers. Exampls: starch, or proteins. Condensation or dehydration reactions create polymers from monomers. TWO MONOMERS ARE JOINED BY REMOVING ONE MOLECULE OF WATER. HYDROLYSIS: when water is added to SPLIT large molecules. Simply the reverse of dehydration synthesis. the 4 different types of Macromolecules!! 1. Carbohydrates
2. Lipids
3. Proteins
4. Nucleic Acids 1. CARBOHYDRATES These include both simple sugars (glucose, fructose, galactose, etc.) and polymers such as starch made from these and other subunits. ALL CARBOHYDRATES EXIST IN A RATIO OF 1 CARBON, 2 HYDROGENS, AND 1 OXYGEN; 1:2:1, or CH2O. examples: glucose C6H12O6 ribose: C5H10O5 MONOSACCHARIDES: are the monomers of carbohydrates. Mono = 1 Poly = many POLYSACCHARIDES: are polymers of monosaccharides examples: starch, glycogen, or cellulose. FUNCTION of POLYSACCHARIDES: ENERGY STORAGE and STRUCTURAL SUPPORT ENERGY STORAGE:
- starch is a storage polysaccharide found in plants (like the potato above)
- glycogen is a storage polysaccharide found in animals, vertabrate muscle, and liver cells. STRUCTURAL SUPPORT:
- Cellulose is a major component of plant cell walls
- Chitin is found in the exoskeleton of arthopods, such as lobsters, and insects and the cell walls of fungi. It gives cockroaches their "crunch". Interesting fact: most biology words ending in "-ose" are sugars like glucose, fructose, lactose, galactose
Rings connect to form polysaccharides (polymer / macromolecule)
2. LIPIDS LIPIDS, are a diverse group of hydrophobic molecules. They aren't polymers per se, as they are assembled from a variety of components. examples include, waxes, oils, fats, and steroids. Fats: (aka triglycerides) are made of a glycerol molecule, and 3 fatty acid molecules. Fatty Acids: contains hydrocarbon chains of variable lengths. the chanins are NONPOLAR, and therefore HYDROPHOBIC 2 types of fatty acids:
1. Saturated fatty acids:
have no bouble bonds between carbons
tend to pack solidly at room temperature
are linked to cardiovascular disease
are commonly produced by animals
examples include butter and lard
2. Unsaturated Fatty Acids:
have some C=C (carbon double bonds); this is what results in the "kinks"
these tends to be liquid at room temperature
commonly produced by plants
Examples include corn oil and olive oil YES, it is as simple as a kink in their chain: Functions of Lipids:
ENERGY STORAGE: FATS STORE TWICE AS MANY CALORIES/GRAMAS CARBOHYDRATES
PROTECTION of vital organs and insulation. In humans and other mammals fat is stored in adipose cells.
PHOSPHOLIPIDS = VERY IMPORTANT!!! They make up cell membranes, the principle behind membrane dynamics is CRUCIAL to the understanding of life as we know it. They have a glycerol backbone (similar to that of triglycerides) which is HYDROPHILIC and have TWO fatty acid tails which are HYDROPHOBIC They are arranged in a bilayer in forming
the cell membrane, of which the hydrophillic
heads point out toward the watery cytosol and
extracellular environment, and hydrophillic
tails are sandwhiched in between Steroids: a very important group of lipids They are made up of 4 rings fused together: examples include... testosterone 3. Proteins amino acid: the building blocks of proteins, there are 22.
They contain a central carbon bonded to a carboxyl group, and amine group, a hydrogen atom, and finally an R group (the variable group or side chain). the different R groups give us different amino acids. Peptide bonds link amino acids. They are formed by DEHYDRATION SYNTHESIS.

THE FUNCTION OF A PROTEIN DEPENDS ON THE ORDER AND NUMBER OF AMINO ACIDS. Primary Structure: The unique sequence the amino acids are joined Secondary Structure: refers to one of the two,3D shapes that
are the result of H-BONDING.
Alpha Helix ( a coil)
Beta Sheet (an accordian)
Tertiary Structure: Results in a complex, globular shape due to the interactions
between R groups: VAN DER WAALS, HYDROPHOBIC INTERACTIONS, H-BONDING,
AND DISULFIDE BRIDGES.

Globular proteins such as ENZYMES, are held in position by these R-group interactions. Quaternary Structure: refers to the association of two or more polypeptide chains into one large protein.

Hemoglobin, is a globular protein with quaternary structure: it is composed of 4 subunits. PROTEIN SHAPE IS CRUCIAL TO PROTEIN FUNCTION!
When a protein does not fold properly, its function is changed. this can be the result of a single aminoacid substitution (more on this later in the genetics unit) Chaperonins: protein molecules that assist in the proper folding of proteins withing cells. They provide an isolating environment in which a polypeptide chain may attain final conformation DENATURATION: this occurs when a protein loses its shape and ability to function. Denaturation commonly happens due to heat, or a change in pH, but other factors can play a part. 4.NUCLEIC ACIDS proteins are polymers made of amino acid monomers! NA store and transmit hereditary information. Examples include: Nucleic acid polymers are made of NUCLEOTIDE monomer units! Nucleotide: made of 3 parts:
1. a Nitrogenous Base Adenine, Guanine, Cytosine, Thymine, and Uracil 2. A Pentose sugar (5 carbon)
(deoxyribose for DNA, ribose for RNA) 3. a Phosphate DNA, is the molecule of heredity
it exists as a double-stranded helix
its nucleotides are adenine, thymine, cytosine, and guanine
Adenines bond with Thymines, while Cytosines bind with Guanines RNA is single stranded. It's nucleotides are adenine, uracil,
cytosine, and guanine. EXIT TICKET!
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