AP Biology: Chapter 5

AP Biology: Chapter 5

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Section 1

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lipids

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Cards (84)

Section 1

(50 cards)

lipids

Front

- diverse group of organic compounds that are insoluble in water but dissolve in nonpolar solvents - do not have true polymers - too small to be considered macromolecules - hydrophobic because they have mostly hydrocarbon regions - varied in form and function - fats, phospholipids, steroids, waxes

Back

enzymatic proteins

Front

- accelerate chemical reactions - digestive enzymes catalyze hydrolysis of food molecules

Back

transport proteins

Front

- transport of substances - hemoglobin transports oxygen from lungs to other parts of body through the bloodstream

Back

aldehyde sugars

Front

- carbonyl group at the end of a carbon skeleton - ex. glyceraldehyde, ribose, glucose, galactose

Back

diversity of polymers

Front

- cells have thousands of different macromolecules - closely related organisms have small differences in polymers (ex. DNA and proteins) - organisms have extensive molecular differences because the diversity of macromolecules is vast and the variety is limitless - there are 40-50 common monomers in which various combinations can be made, thus creating diversity - polymers are made up different monomers and arranged in various ways - small molecules are common to all organisms but ordered into unique macromolecules - despite diversity, members of each of the 4 classes of macromolecules are similar in structure and function

Back

saturated fatty acids

Front

- a fatty acid with no carbon double bonds - maximum amount of hydrogen bonded to the carbon skeleton, so it is saturated - solid at room temperature - straight chain - most animal fats are saturated and flexibility allows tight packing - ex. bacon grease, butter

Back

enzyme

Front

a specialized protein macromolecule that speeds up chemical reactions

Back

triacylglycerol

Front

a fat composed of three fatty acids bonded to one glycerol by ester linkages

Back

fats and diet

Front

- diet rich in saturated fats can contribute to cardiovascular diseases such as atherosclerosis - plaque deposits develop within walls of blood vessels and bulge inwards - impedes blood flow and reduces vessels' relsilience

Back

trioses

Front

- sugars that have three carbons - glyceraldehyde, dihydroxyacetone

Back

storage polysaccharides

Front

- plants and animals store sugars for later use in the form of storage polysaccharides - starch is stored in plants and can be withdrawn by hydrolysis - glycogen is stored in animals and used for short term storage

Back

unsaturated fatty acids

Front

- a fatty acid with one or more carbon double bonds - for every double bond, there is fewer hydrogen bonds - liquid at room temperature - double bonds cause kinks, or bends, in the chain - most plant fats - ex. olive oil, corn

Back

dehydration reaction

Front

- a reaction where polymers are synthesized - two molecules are covalently bonded to each other - a water molecule is lost - each monomer contributes part of the water molecule during the reaction: one provides hydroxyl (OH), the other provides hydrogen (H) - repeats to create longer chains, or polymers - requires energy and biological catalysts - a.k.a dehydration synthesis or condensation

Back

polypeptide

Front

a polymer of many amino acids linked by peptide bonds that makes up proteins

Back

amino acid

Front

- an organic molecule with both an amino group and a carboxyl group - amino group: NH₂ (left) - alpha (α) carbon in center that connects to four different partners - hydrogen atom (bottom) - carboxyl group: COOH (right) - R group, or side chain (top) - physical and chemical properties of the side chain determine the characteristics of the amino acid - amino groups and carboxyl grouups are usually ionized at the pH level in the cell

Back

trans fat

Front

- unsaturated fats that have been altered through hydrogenation so that instead of cis bonds, the hydrogen forms trans bonds - chain is straight because of trans bonds - may contribute more than saturated fats to disease

Back

peptide bond

Front

a covalent bond between amino acids that makes up polypeptides through dehydration reactions

Back

monomer

Front

- the repeating units that serve as the building blocks of a polymer that are smaller molecules - have other functions of their own

Back

disaccharide

Front

- a double sugar that consists of two monosaccharides joined by a glycosidic linkage - maltose: glucose + glucose; malt sugar in brewing beer - sucrose: glucose + fructose; table sugar and used to transport carbohydrates from leaves to roots in plants (most prevalent disaccharide) - lactose: glucose + galactose; milk sugar

Back

polymer

Front

- a long molecule consisting of many similar or identical building blocks/subunits linked by covalent bonds - carbohydrates, proteins, and nucleic acid macromolecules all form chains of polymers - made out of monomers

Back

storage proteins

Front

- storage of amino acids - casein, protein of milk, is a source of amino acids for baby mammals

Back

fats

Front

- large molecules assembled from glycerol and fatty acids by a dehydration reaction - major function is energy storage - gram of fat stores more than twice as much energy as a gram of a polysaccharidie - less bulky and allow animals to carry energy in a compact reservoir via adipose cells that shrink and swell as fat is added or removed - adipose tissue cushions organs and insulated the body - hydrophobic because they have hydrocarbon chains of fatty acids - separate from water because the water hydrogen-bonds with itself and excludes fat - composed of three fatty acid molecules that are joined to glycerol by an ester linkage: results in a triacylglycerol - can be three different fatty acids or the same - saturated, unsaturated, or trans

Back

fatty acid

Front

- a smaller molecule that has a long carbon skeleton (16-18 carbons) - carbon at one end is part of a carboxyl group - rest of the skeleton is a hydrocarbon chain - nonpolar C-H bonds make it hydrophobic

Back

structural proteins

Front

- support - keratin supports hair

Back

defensive proteins

Front

- protection against disease - antibodies destroy viruses

Back

hydrolysis

Front

- a reaction where polymers are broken down - bond between monomers is broken - a water molecule is added - hydrogen (H) attaches to one monomer and hydroxyl (OH) attaches to the other monomer - ex. digestion: organic material in good is too large to enter cells, so enzymes attack polymers and speed up hydrolysis; released monomers can be absorbed into the bloodstream and dehydration can be used to form new specialized polymers for the cell

Back

macromolecules

Front

- a giant molecule formed by the joining of smaller molecules, usually by a dehydration reaction - carbohydrate, protein, or nucleic acid (lipids do not include true polymers and generally too small to be classified as a macromolecule) - relatively large - may consist of thousands of covalently bonded atoms and have a mass more than 100,000 daltons - very complex and have a detailed structure - architecture plays an essential role in function - exhibit unique emergent properties that arise from the orderly arrangement of their atoms

Back

polysaccharides

Front

- macromolecules and polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages - storage material and hydrolyzed as needed to provide sugar for cells (starch in plants and glycogen in animals) - building material for structures that protect the cell or the whole organism (cellulose in plants and chitin in arthropods) - architecture and function determined by the sugar monomers and position of the glycosidic linkages

Back

proteins

Front

- a biologically functional molecule that is made up of one or more polypeptides that is folded into a specific three-dimensional structure - humans have tens of thousands of proteins which have different structures and functions - constructed from the same set of 20 amino acids - 50% of dry mass of most cells - most important macromolecule, instrumental in everything organisms do

Back

pentoses

Front

- sugars that have five carbons - ribose, ribulose

Back

contractile and motor proteins

Front

- movement - motor proteins cause undulations of cilia and flagella - actin and myosin cause muscle contraction

Back

protein functions

Front

- enzymes - defense - storage - transport - hormonal - receptor - contractile and motor - structural

Back

glycogen

Front

- polymer of glucose - extensively branched - stored in liver and muscle cells in vertebrates - hydrolysis in cells release glucose when demand increases - cannot sustain long-term - depleted in about a day until replenished by consumption of food - low-carb diets result in weakness

Back

hormonal proteins

Front

- coordinate organism's activities - insulin causes tissues to take up glucose and regulates the blood sugar concentration

Back

ketone sugars

Front

- carbonyl group within carbon skeleton - ex. dihydroxyacetone, ribulose, fructose

Back

hexoses

Front

- sugars that have six carbons - glucose, fructose, galactose

Back

structural polysaccharides

Front

- polysaccharides which organisms build strong materials from - cellulose in plants is part of plant cell enclosures - chitin in arthropods is used for their exoskeletons

Back

carbohydrates

Front

- macromolecules that serve as fuel and building material - energy used right away, easier to use and with less energy (short-term) - include sugars and their polymers - polymers made by dehydration - classified by the number of simple sugars - can be monosaccharides, disaccharides, or polysaccharides

Back

characteristics of sugar

Front

- carbonyl group (CO) which oxygen is double bonded to carbon - multiple hydroxyl groups (OH) attached to each carbon except one - either an aldose (aldehyde sugar) or a ketose (ketone sugar) - size of carbon skeleton can range from 3 to 7 carbons long - spatial arrangement around asymmetric carbons can vary (enantiomers: glucose and galactose), causing different biochemical properties - form rings in aqueos solutions

Back

phospholipids

Front

- a type of lipid similar to a fat molecule but has only two fatty acids attached to glycerol, and the third hydroxyl group of glycerol is attached to a negatively charged phosphate - two ends show different behavior to water: hydrocarbon tails are hydrophobic; phosphate group forms a hydrophilic head that has an affinity for water - assembles into bilayers and shields the hydrophobic portions from water - arranged in a similar bilayer in cells as the hydrophilic heads is on the outside that makes contact with substances and the hydrophobic head is on the inside - bilayer separates the cell and the environment - ex. choline

Back

catalysts

Front

- chemical agents that selectively speed up chemical reactions without being consumed by the reaction - regulate metabolism - most enzymes are proteins

Back

receptor proteins

Front

- response of cell to chemical stimuli - receptors in nerve cell membrane detect signaling molecules from other nerves

Back

monosaccharides

Front

- simple sugars - generally have molecular formulas that are some multiple of the unit CH₂O - the most common monosaccharide is glucose (C₆H₁₂O₆) - major nutrients for cells, particularly glucose - can be produced by photosynthetic organisms - store energy in chemical bonds which can be harvested by cellular respiration, a process where cells extract energy by breaking molecules down in a series of reactions - carbon skeletons are raw material for the synthesis of other organic molecules (ex. amino acids, fatty acids) - can be incporated as monomers in disaccharides and polysaccharides

Back

glycosidic linkage

Front

- a covalent bond formed between two monosaccharides by a dehydration reaction - the hydroxyl of one monosaccharide bonds with the hydrogen of the hydroxyl of another monosaccharide, which forms H₂O - the remaining oxygen molecule links the two monomers - alpha (α) or beta (β) ring forms - different links give distinct three-dimensional shapes

Back

ester linkage

Front

a bond formed by a dehydration reaction between a hydroxyl group and a carboxyl group that produces a triacylglycerol

Back

starch

Front

- a polymer of glucose monomers - alpha (α) ring forms: the hydroxyl group attached to the number one carbon is below the plane of the ring (all on the same side) - helical - a storage polysaccharide - in the form of granules within cellular structures called plastids that have chloroplasts - synthesis enables accumulation of glucose - represents stored energy - sugar can be withdrawn from starch by hydrolysis, which breaks glucose monomer bonds - humans and other animals have enzymes that hydrolyze plant starch for nutrients - glucose, monomers in starch, usually joined by 1-4 linkages - amylose, the simplest starch, is unbranched - amlyopectin, a complex starch, is branched with 1-6 linkages

Back

steroids

Front

- lipids that have a carbon skeleton of four fused rings which have various chemical groups attached to it - chemical messengers and send chemical signals to cells - ex. cholesterol: steroid molecule that is in cell membranes and precursor of sex hormones and other molecules - saturated fats and trans fats affect cholesterol levels which can contribute to cardiovascular disease

Back

chitin

Front

- a structural polysaccharide - carbohydrate used by arthropods to build exoskeletons - embedded in a layer of proteins so the exoskeleton is leathery and flexible initially, and then hardened as proteins are linked and calcium carbonate encrusts it - found in fungi as a replacement for cellulose - similar to cellulose but has a nitrogen-containing appendage in glucose

Back

4 major classes of large biological molecules

Front

carbohydrates, lipids, proteins, nucleic acids

Back

cellulose

Front

- a structural polysaccharide in plants which is a polymer of glucose - major component of tough cell walls in plants - beta (β) ring forms: the hydroxyl group attached to the number 1 carbon is upside down compared to its adjacent glucose monomer (alternating sides) - straight and never branched - hydroxyl groups can bond with parallel cellulose which creates groups called microfibrils, strong building material and part of paper and cotton - enzymes cannot break down both alpha and beta links; few organisms can digest cellulose and eliminated as feces - part of a healthy diet; abrades digestive tract and causes mucus secretion - most abundant organic compound on Earth: over 100 billion tons produced each year

Back

Section 2

(34 cards)

genomics and proteomics to evolution

Front

- closely related species have more similar sequences of DNA and amino acids, than more distantly related species - using this type of molecular evidence, biologists can deduce evolutionary relationships among species - DNA passed down determine amino acid sequences which determine similarity in proteins

Back

deoxyribonucleic acid (DNA)

Front

- a nucleic acid that contains coded information that programs all cell activity - contains directions for self-replication - is copies and passed down from generations (inherited) - found in the nucleus of eukaryotic cells - makes up genes that have instructions for RNA and protein synthesis - very long, consisting of hundreds to more than a thousand genes - not directly involved in running operations - adenine, guanine, cytosine, thymine - deoxyribose - double helix and needs compatible bases

Back

proteomics

Front

the analysis of large sets of proteins and their sequences

Back

double helix

Front

- a shape where strands wind around an imaginary axis - DNA

Back

ribose

Front

- the sugar in RNA - has an oxygen atom on the second carbon on the ring

Back

tertiary structure

Front

- the oversall shape of a polypeptide resulting from the interactions between the side chains of the various amino acids - hydrophobic interaction: hydrophobic amino acids cluster at the core, away from water - van der Waals interactions: hold the nonpolar side chains together - hydrogen bonds and ionic bonds: connect different parts of the side chain and stabilize it - disulfide bridges: covalent bonds that further reinforce shape of a protein; two cysteine monomers with sulfhydryl groups from a bond with two sulfurs

Back

secondary structure

Front

- segments of chains that are repeatedly coiled and folded as a result of hydrogen bonds - the weakly positive hydrogen atom attached to the nitrogen atom has an affinity for the oxygen atom of a nearby peptide bond. - each hydrogen bond is weak, but the sum of many hydrogen bonds stabilizes the structure of part of the protein - α helix: delicate coil held together by hydrogen bonding every 4th amino acid - β pleated sheet: two or more segments of polypeptide chain lying side by side, so hydrogen bonds between the parts can form and hold it together

Back

gene

Front

- a discrete unit of inheritance that programs the amino acid sequence of a polypeptide - consists of DNA

Back

quaternary structure

Front

- the overall protein structure that results from the aggregation of the polypeptide subunits - the association of two or more polypeptides

Back

base pairing in RNA

Front

- adenine with uracil - cytosine with guanine - allows it to take 3-D shape

Back

nucleotides

Front

- monomers that make polynucleotides - composed of a pentose, a five-carbon sugar, a nitrogen-containing (nitrogenous) base, and one or more phosphate groups - nucleoside: portion of a nucleotide without phosphate

Back

bioinformatics

Front

the use of computer software and other computational tools that can handle and analyze large data sets

Back

nucleic acid

Front

- polymers made of monomers called nuleotides - DNA or RNA - macromolecules as polynucleotides - determines protein structure

Back

Frederick Sanger and his research

Front

- pioneer in determining the amino acid sequence of proteins - worked in Cambridge University, England in the 1940s to 1950s\ - used agents to break down insulin polypeptides into parts - used chemical methods to analyze amino acid sequence of smaller parts - reconstructed complete amino acid of insulin - steps in sequencing since then have been automated

Back

polypeptide chain

Front

- polymers of amino acids that are arranged in a specific linear sequence and are linked by peptide bonds - the repeating sequence of atoms that groups are attached to is called the polypeptide backbone - different side chains are attached to the backbone - one end of the chain has a free amino group (NH₂) and the other end has a free carboxyl group (COOH); any polypeptide has an amino end (N-terminus) and a carboxyl end (C-terminus)

Back

primary structure

Front

- a protein's sequence of amino acid - inherited by genetic information - dictates secondary and tertiary structure due to the chemical nature of the backbone and side chains

Back

protein structure

Front

- a functional protein is one or more polypeptides precisely twisted, folded, and coiled into a unique shape - amino acid sequence determines structure and shape - formation of bonds allows spontaneous folding - globular or fibrous - enables recognition and ability to bind to other molecules - dependent on the physical and chemical conditions of the protein's environment: pH, salt concentration, temperature - four levels of protein structure: primary, secondary, tertiary, quaternary

Back

denaturation

Front

- a process where a protein unravels and loses its native shape - caused by changes in environment: pH, salt concentration, temperature - weak chemical bonds and interactions are destroyed - usually happen when transferred from aqueous to nonpolar solvent

Back

gene expression

Front

- a process where DNA directs RNA synthesis, which controls protein synthesis - mRNA is synthesized in the nucleus and moved into the cytoplasm via nuclear pore - protein is synthesized using information in the mRNA

Back

ribosomes

Front

- sites of protein synthesis - in eukaryotic cells, ribosomes are in between the nucleus and cytoplasm

Back

pyramidines

Front

- one of the families of nitrogenous bases that has one six-membered ring of carbon and nitrogen atoms - cytosine, thymine, uracil

Back

deoxyribose

Front

- the sugar in DNA - lacks an oxygen atom on the second carbon on the ring

Back

sugar-phosphate backbone

Front

- a repeating pattern of sugar-phosphate units where adjacent nucleotides are joined by a phosphodiester linkage - one end has a phosphate attached to the 5' carbon while the other end has a hydroxyl group on a 3' carbon (5' end 3' end) - has nitrogenous bases as appendages along the backbone

Back

base pairing in DNA

Front

- adenine with thymine - cytosine with guanine

Back

chaperonins

Front

- protein molecules that assist in the proper folding of other proteins - keep the new polypeptide segregated from chemical conditions in the cytoplasm as it folds - provides shelter and ensures beneficial hydrophilic environment - misfolding of polypeptides can cause diseases such as cystic fibrosis, Alzheimer's, and Parkinson's

Back

X-ray crystallography

Front

- a process used to determine the 3-D structure of many proteins

Back

antiparallel

Front

- when two things run in opposite directions from each other but parallel - two strands of DNA run in opposite 5'-3' directions

Back

Human Genome Project

Front

- a project where biologists sequences the entire human genome from 1990 to 2000s - sequences all 3 billion bases - drastically reduced time now

Back

ribonucleic acid (RNA)

Front

- a nucleic acid that functions in the actual synthesis of proteins coded for by DNA - mRNA: messenger RNA that interacts with the cell's protein-synthesizers to direct production - conveys genetic information from nucleus to cytoplasm - adenine, guanine, cytosine, uracil - ribose - single strands - versatile

Back

20 amino acids

Front

- hydrophobic/nonpolar: glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, trptophan, proline - polar/hydrophilic: serine, threonine, cysteine, tryosine, asparagine, glutamine - electrically charged/hydrophilic: aspartic acid, glutamic acid, lysine, arginine, histidine

Back

polynucleotides

Front

- polymers that nucleic acids exist as - made up of monomers called nucleotides

Back

genomics

Front

the analysis of large sets of genes or comparing whole genomes of different species

Back

sickle-cell disease

Front

- an inherited blood disorder caused by the substitution of valine for glutamic acid in hemoglobin - sickle-shaped hemoglib molecules - cells clog blood vessels and impede flow - shows that slight change can affect function

Back

purines

Front

- one of the families of nitrogenous bases that has one-six membered ring of carbon and nitrogen attached to a five-membered ring - adenine, guanine

Back