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ลำดับตอนที่ #9 : [[R.S.]]AP Biology Test::Chapter.5::8.10.09

review sheet of AP Biology for

Chapter 5* 8.Oct.09

 

Chapter.5 :: The Structure and Function of Macromolecules  [[Page.68]]

Overview ‘The Molecules of Life’ [[Page.68]]

-          Another level in hierarchy of biological organization is reached when small organic molecules are joined inside cells, forming larger molecules.

-          The 4 main classes of large biological molecules are carbohydrates, lipids, proteins, nucleic acids. 

·         Biologists use the term macromolecule for such giant molecules.  

Concept 5.1 – Most macromolecules are polymers, built from monomers [[Page.68]]

-          Three of the four classes of macromolecules – carbohydrates, proteins, and nucleic acids – are chain-like molecules called polymers.

·         A polymer is a long molecule consisting of many similar or identical building blocks linked by covalent bonds.

·         The repeating units that serve as the building blocks of a polymer are small molecules called monomers. (some monomers have other functions of their own)

-          Polymeric macromolecules are different in their monomers but the chemical mechanisms by which cells make and break polymers are basically the same in all cases.

-          Monomers are connected by a reaction in which two molecules are covalently bonded to each other through loss of a water molecule; this is called a condensation reaction, or a dehydration reaction, because the molecule lost is water.

·         When a bond forms between two monomers, each monomer contributes part of the water molecule that is lost: One molecule provides a hydroxyl group (--OH), while the other provides a hydrogen (--H).

·         Cell must expend energy to carry out dehydration reactions, and the process occurs only with the help of enzymes, specialized proteins that speed up chemical reactions in cells.

-          Polymers are disassembled to monomers by hydrolysis, a process that is essentially the reverse of the dehydration reaction.

·         Bonds between monomers are broken by the addition of water molecules, a hydrogen from the water attaching to one monomer and a hydroxyl group attaching to the adjacent monomer.

-          For example, when our food is taken in as organic polymers that are too large for our cells to absorb. Within the digestive tract, various enzymes direct hydrolysis of specific polymers and the results are monomers that could be absorbed to the bloodstream. The body cells then use dehydration reaction to assemble the monomers into new, different polymers.

-          Each cell has thousands of different kinds of macromolecules; those molecules vary among cells of the same individual, vary more among unrelated individuals of species, and vary even more between species.

·         This diversity comes from various combinations of 40 – 50 common monomers and some others that occur rarely. They can be connected in many combinations (with different arrangement)

Concept 5.2 – Carbohydrates serve as fuel and building material [[Page.69]]

-          Carbohydrates include both sugars and the polymers of sugars.

·         Monosaccharides, or simple sugars, are the simplest carbohydrates.

·         Disaccharides, or double sugars, consisting of 2 monosaccharides joined by a condensation reaction.

·         Polysaccharides are polymers of many monosaccharides (they are macromolecules)

1.       Monosaccharides generally have molecular formulas that are some multiple of the unit CH₂O. Ex. glucose – the most common monosaccharide – has the formula  C₆H₁₂O₆

1.1   Glucose [reserved energy in our bodies]

1.2   Fructose [fruit sugar]

1.3   Galactose [milk sugar]

·         They have a carbonyl group (>C=O) and multiple hydroxyl group (--OH); depending on the location of the carbonyl group, the sugar is an aldose (aldehyde sugar) or a ketose (ketone sugar).

ð Ex. Glucose (an aldose) and fructose (a ketose) are structural isomers.

·         Most names for sugars end in –ose. 

·         Monosaccharides can also be classified by the number of carbons in carbon skeleton.

ð Ex. Glucose are hexoses (6-carbon sugar),, pentoses and trioses are also common.

·         They may exist as enantiomers (Ex. Glucose and galactose = both are hexoses aldoses but they are differ in the spatial arrangement of their parts around asymmetrical carbons)

·         Glucose molecules, as well as other sugars, form rings in aqueous solutions.

·         Monosaccharides , particularly glucose, are major nutrients and fuel for cells.

ð In the process of cellular respiration, cells extract the energy stored in glucose molecules. Their carbon skeletons serve as raw material for the synthesis of other monomers (such as amino acids & fatty acids) as well.

2.       Disaccharide consists of two monosaccharides joined by a glycosidic linkage, a covalent bond formed between two monosaccharides by a dehydration reaction.

2.1   Maltose (Glucose + Glucose)

2.2   Sucrose (Fructose + Glucose) = most prevalent disaccharide 

2.3   Lactose (Galactose + Glucose) = animal milk

·         All of them have the formula of C₁₂H₂₂O₁₁ (since during the reaction, C₁₂H₂₄O₁₂ releases H₂O)

3.       Polysaccharides are macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages.

·         Some polysaccharides serve as storage material, hydrolyzed as needed to provide sugar for cells. Others serve as building material for structures that protect the cell or the whole organism.

·         Their functions are determined by the sugar monomers & positions of glycosidic linkages

3.1   Starch, a storage polysaccharide of plants, is a polymer consisting entirely of glucose monomers. Most of those monomers are joined by 1-4 linkages (number 1 carbon to number 4 carbon).

ð The simplest form of starch, amylase, is unbranched and forms a helix.

ð Plants store starch as granules within cellular structures called plastids, which include chloroplasts. Synthesizing starch enables plant to stockpile surplus glucose. Those sugars can later be withdrawn by hydrolysis as well.

3.2   Glycogen is a polysaccharide that animals store; it is a polymer of glucose that is like amylopectin but more extensively branched.

ð Humans + other vertebrates store a day’s supply of glycogen in the liver & muscles.

3.3   Cellulose is a major component of tough walls that enclose plant cells; it is the most abundant organic compound on Earth. (structural polysaccharide)

ð Like starch, cellulose is a polymer of glucose. However, the glycosidic linkages in these two polymers are different. This difference is based on the two slightly different ring structures for glucose … these two rings form differ in whether the hydroxyl group attached to the number 1 carbon is fixed above (beta glucose) or below (alpha glucose) the plane of the ring.

ð The glucose monomers of cellulose are in the beta configuration, making every other glucose monomer upside down with respect to its neighbors.

ð The straight structures built with beta glucose in cellulose allow H atoms on one strand to form hydrogen bonds with OH groups on other hands.

ð In plant cell walls, parallel cellulose molecules held together in this way are grouped into units called microfibrils, which form strong building materials for plants (and for humans, as lumber)

ð The enzymes that digest starch by hydrolyzing its alpha linkages cannot hydrolyze the beta linkages in cellulose.

~ Cellulose in human food passes through the digestive tract and is eliminated in feces as ‘insoluble fiber.’ (Human can’t digest cellulose)

~ Many eukaryotic herbivores, from cows to termites, as well as some fungi can digest cellulose and break it down to glucose monomers

3.4   Chitin is carbohydrate used by arthropods (insects, spiders, crustaceans, and related animals) to build their exoskeletons, which are hard case that surround the soft parts of those animals. (Chitin is another important structural polysaccharide)

ð It is similar to glucose except that it contains a nitrogen-containing appendage on each glucose monomer.

Concept 5.3 – Lipids are a diverse group of hydrophobic molecules [[Page.74]]

-          Unlike other macromolecules, lipids do not form polymers.

-          The compounds called lipids are grouped together because they share one important trait: They have little or no affinity for water (they are hydrophobic)

·         This is because they consist mostly of hydrocarbons, which form nonpolar covalent bond.

-           Lipids are highly diverse in form and function.

-          The most biologically important types of lipids are fats, phospholipids, and steroids.

1.       A fat is constructed from two kinds of smaller molecules: glycerol and fatty acids.

ð Glycerol is an alcohol with three carbons, each bearing a hydroxyl group

ð A fatty acid has a long carbon skeleton, usually 16 or 18 carbon atoms in length

·         Fats are not polymers but they are large molecules and are assembled from smaller molecules by dehydration reaction.

·         The nonpolar C – H bonds in the hydrocarbon chains of fatty acids are the reason fats are hydrophobic. Fats separate from water because the water molecules hydrogen-bond to one another and exclude the fats.

·         In a fat, 3 fatty acids are joined to glycerol by an ester linkage (a bond between a hydroxyl group & carboxyl group), creating a triacylglycerol, or triglyceride.  

ð The 3 fatty acids can be the same or different.

·         Fatty acids may vary in length (number of carbons) and in the number & locations of the double bonds.

ð If the fatty acid has no carbon-carbon double bonds in the hydrocarbon chains, then the molecule is a saturate fatty acid since it is saturated with hydrogens at every possible position.

ð If the fatty acid has one or more carbon-carbon double bonds formed by the removal of hydrogen atoms from the carbon skeleton, then the molecule is an unsaturated fatty acid. 

·         A saturated fatty acid is a straight chain, but an unsaturated fatty acid has a kink (ปม) wherever there is a double bond.

1.1   Fats made from saturated fatty acids are saturated fat.

Most animal fats are saturated and they are solid at room temperature due to the tightly pack molecules that lack double bounds.

ð A diet rich in saturated fats may contribute to cardiovascular disease like atherosclerosis through plaque deposits

1.2   Fats made from unsaturated fatty acids are unsaturated fat.

Fats of plants and fishes (oils) are unsaturated and usually they are liquid at room temperature since the kinks caused by double bonds prevent molecules from packing tightly enough to solidify.

ð The phrase ‘hydrogenated vegetable oils’ means that unsaturated fats have been synthetically converted to saturated fats by adding hydrogen.

ð The process of hydrogenated vegetable oils produces saturated fats and also unsaturated fats with trans double bonds. These trans fat molecules contribute more than saturated fats to atherosclerosis.

·         The major function of fats is energy storage.

ð A gram of fats store more than twice as much energy as a gram of a polysaccharide, such as starch.

ð Because plants are immobile, they can function with bulky energy storage in the form of starch. Plants use oils when dispersal and compact storage is important, as in seeds.

ð Animals must carry their energy stores with them and benefit from having a more compact fuel reservoir of fat.

ð Humans and other mammals store fats as long-term energy reserves in adipose cells that swell and shrink as fat is deposited or withdrawn from storage.

2.       A phospholipidis similar to fat but has only 2 fatty acids attached to glycerol rather than 3. The third hydroxyl group of glycerol is joined to a phosphate group, which has a negative electrical charge.

·         Additional small molecules, usually charged ore polar, can be linked to the phosphate group to form a variety of phospholipids. 

·         Phospholipids interaction with water :: their hydrocarbon tails are hydrophobic and are excluded from water but their phosphate group and its attachments form a hydrophilic head. So, when they are added to water, they self-assemble into double-layered aggregates – bilayers – with the hydrophobic tails pointing toward the interior.

ð This type of structure is called a micelle.

·         Phospholipids are arranged as a bilayer at the surface of a cell as well. It forms a barrier between the cell and the external environment.

ð Phospholipids are the major component of cell membranes.

3.       Steroids are lipids characterized by a carbon skeleton consisting of four fused rings. (different steroids vary in the functional groups attached to this ensemble of rings)

·         Cholesterol, an important steroid, is a common component of animal cell membranes and is also the precursor from which other steroids are synthesized

(ex. Vertebrate sex hormones)

ð However, high levels of cholesterol in the blood may contribute to cardiovascular disease (atherosclerosis)  

Concept 5.4 – Proteins have many structures, resulting in a wide range of functions [[Page.74]]

-          Proteins account for more than 50% of the dry mass of most cells, and they are instrumental in almost everything organisms do.

-          Some proteins speed up chemical reactions, while others play a role in structural support, storage, transport, cellular communications, movement, and defense against foreign substances. 

Type of Protein	Function	Examples
Enzymatic proteins	Selective acceleration of chemical reactions	Digestive enzymes
Structural proteins	Support	Collagen, elastin, keratin
Storage proteins	Storage of amino acids	Ovalbumin, casein
Transport proteins	Transport of other substances	Hemoglobin
Hormonal proteins	Coordination of an organism’s activities	Insulin
Receptor proteins	Response of cell to chemical stimuli	Receptors -_-
Contractile & motor proteins	Movement	Actin, myosin
Defensive proteins	Protection against disease	Antibodies

-          The most important type of protein may be enzymes. Enzymatic proteins regulate metabolism by acting as catalysts, chemical agents that selectively speed up reactions in the cell without being consumed by the reaction.

-          Human has tens of thousands of different proteins, each with a specific structure and function; proteins, in fact, are the most structurally sophisticated molecules known.

-          Each type of protein has a complex three-dimensional shape, or conformation.

-          All protein polymers are constructed from the same set of 20 amino acid monomers.

·         Polymers of proteins are called polypeptides.

-          A protein consists of one or more polypeptides folded & coiled into specific conformations

-          Amino acids are organic molecules possessing both carboxyl & amino groups. At the center of amino acid is an asymmetric carbon atom called the alpha carbon. Its four components partners are an amino group, a carboxyl group, a hydrogen atom, and the R group (side chain), which differs with each amino acid.

·    Nonpolar amino acids :: Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Methionine, Proline, Tryptophan

·    Polar amino acids :: Serine, Theonine, Tyrosine, Cystenine, Asparagine, Glutamine

·    Elctrically charges ::

ð Acidic :: aspartic acid, glutamic acid

ð Basic :: Histidine, Lysine, Arginine

-          The physical and chemical properties of the side chain determine the unique characteristics of a particular amino acid.

·    One group has nonpolar & hydrophobic R groups

·    Another group has polar & hydrophilic R groups

·         A third group of amino acids includes those with functional groups that are charged (ionized) at cellular pH. Some acidic R groups are negative in charge due to presence of a carboxyl group. Basic R groups are positive in charge.

-         Amino acids are joined together when a dehydration reaction removes a hydroxyl group from the carboxyl end of one amino acid & a hydrogen from the amino group of another.

·         The resulting covalent bond is called a peptide bond.

·         Repeating this process over and over creates a polypeptide chain.

ð At one end is an amino acid with a free amino group (the N-terminus) and at the other is an amino acid with a free carboxyl group (the C-terminus)

ð The repeating sequence of atoms in polypeptide is polypeptide backbone.

·         Polypeptides range in length from a few monomers to a thousand or more.

·         Each specific polypeptide has a unique linear sequence of amino acids.

-         Frederick Sanger determined the amino acid sequence of insulin in 1950s by using protein-digesting enzymes & other catalysts to break polypeptides of insulin at specific places.

·         The fragments were separated by technique called chromatography

·         Hydrolysis by another agent broke the polypeptide at different sites, yielding a second group of fragments. The chemical methods are then used to determine to sequence of amino acids in those small fragments.

·         The overlapping regions among pieces obtained are searched, so Sanger was able to reconstruct the complete primary structure of insulin.

-         A functional protein is not just a polypeptide chain, but one or more polypeptides precisely twisted, folded, and coiled into a molecule of unique shape.

-         It is the amino acid sequences of a polypeptide that determines what three-dimensional conformation the protein will take.

-         When a cell synthesizes a polypeptide, the chain generally folds spontaneously, assuming the functional conformation for that protein. This folding is driven and reinforced by the formation of a variety of bonds between parts of the chain, which in turn depends on the sequence of amino acids.

·         Many proteins are globular (roughly spherical), while others are fibrous in shape.

-         A protein’s specific conformation determines how it works.

-         In almost every case, the function of a protein depends on its ability to recognize and bind to some other molecule.

·         An antibody binds to a particular foreign substance that has invaded the body

·         An enzyme recognizes and binds to its substrate, the substance that enzymes work on

·         Natural signal molecules called endorphins bind to specific receptor proteins on the surface of brain cells in humans, producing euphoria and relieving pain.

ð Morphine, heroin, and other opiate drugs mimic endorphins because they are similar in shape and can bind to the brain’s endorphin receptors.

-         In the complex architecture of a protein, we can recognize three superimposed levels of structure, known as primary, secondary, and tertiary structure. A fourth level, quaternary structure, arises when a protein consists of two or more polypeptide chains.

1.       The primary structure of a protein is its unique sequence of amino acids. It is like the order of letters in a very long word and its structure is not determined by random linking of amino acids, but by inherited genetic information.

·         Even a slight change in this structure can affect a protein’s conformation and ability to function.

ð The substitution of one amino acid (valine) for the normal one (glutamic acid) at a particular position in primary structure of hemoglobin, the protein that carries oxygen to red blood cells, can cause sickle-cell disease, an inherited blood disorder. 

2.       Most proteins have segments of their polypeptide chains repeatedly coiled or folded. These coils and folds are referred to as secondary structure which is the result from hydrogen bonds between the repeating constituents of polypeptide backbone.

·         The weakly positive hydrogen atom attached to the nitrogen atom has 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 protein.

·         Typical secondary structures are coils (an alpha helix) or folds (beta pleated sheets)

3.       Tertiary structure is the overall shape of a polypeptide resulting from interactions between the R groups of the various amino acids.

·         These interactions include hydrogen bounds between polar and/or charge areas, ionic bonds between charged R groups, and hydrophobic interactions and van der Waals interactions among hydrophobic R groups.

·         While these three interactions are relatively weak, strong covalent bonds called disulfide bridges that form between the sulfhydryl groups (--SH) of two cysteine monomers act to rivet parts of the protein together.

4.       Quaternary structure is the overall protein structure that results from the aggregation of these polypeptide subunits.

·         Ex. Collagen = a fibrous protein of three polypeptides that are supercoiled like rope ,,

      Hemoglobin = globular protein which consists of four polypeptide subunits: two alpha and two beta chains.

-         Key factors that determine protein conformation …

·         A polypeptide chain of a given amino acid sequence can spontaneously arrange itself into a 3D shape determined and maintained by the interactions responsible for secondary and tertiary structure. This folding occurs as the protein is being synthesized within cells.

·         Physical and chemical conditions of the protein’s environment.

ð Alteration in pH, salt concentration, temperature, or other factors can unravel and lose its native conformation, this change is called denaturation.

ð Most protein become denatured if they are transferred from an aqueous environment to an organic solvent. Other denaturation agents include chemicals that disrupt the hydrogen bonds, ionic bonds, and disulfide bridges that maintain a protein’s shape. Denaturation can also be caused by excessive heat, which disrupts weak interactions that stabilize conformation.

ð Some proteins can return to its functional shape when the denaturing agent is removed but some, esp. ones in crowded environment inside cells, cannot.

-         Biochemists find it difficult to predict the conformation of a protein from its primary structure alone because most proteins appear to undergo several intermediate stages of folding before reaching their ‘mature’ conformation.

·         Instead, researchers discovered chaperonins which are protein molecules that assist the proper folding of other proteins. They work by keeping the new polypeptide segregated from bad influences in the cytoplasmic environment while it folds spontaneously.

·         At present, scientists use X-ray crystallography to determine protein three-dimensional structure (conformation); this requires the formation of a crystal of the protein being studied

·         Another method is nuclear magnetic resonance (NMR) spectroscopy, which does not require protein crystallization.

Concept 5.5 – Nucleic acids store and transmit hereditary information [[Page.86]]

-         The amino acid sequence of a polypeptide in protein’s primary structure is programmed by a unit of inheritance known as gene.

·         Genes consist of DNA, which is a polymer known as nucleic acids.

-         There are 2 types of nucleic acids: deoxyribonucleic acid (DNA) & ribonucleic acid (RNA)

·         These are the molecules that enable living organisms to reproduce their complex components from one generation to the next.

ð DNA provides directions for its own replication and it also directs RNA synthesis and, through RNA, controls protein synthesis.

-         DNA is the genetic material that organisms inherit from their parents.

·         Each chromosome contains one long DNA molecule, usually consisting of from several hundred to more than a thousand genes.

·         When a cell reproduces itself by dividing, its DNA molecules are copied & passed along from one generation of cells to the next.

-         While DNA encodes the information that programs all the cells activities, proteins are responsible for implementing the instructions contained in DNA.

-         Each gene along the length of DNA molecule directs the synthesis of a type of RNA called messenger RNA (mRNA). The mRNA molecule then interacts with the cells’ protein-synthesizing machinery to direct the production of polypeptide.

-         The flow of genetic information is from DNA => RNA = > protein.

·         The actual sites of protein synthesis are cellular structures called ribosomes.

ð in eukaryote = ribosomes in cytoplasm & DNA in nucleus (mRNA conveys genetic instruction for building proteins from nucleus to cytoplasm)

ð in prokaryote = lack nuclei but use RNA to send message from DNA to ribosomes

-         Nucleic acids are macromolecules that exist as polymers called polynucleotides.

·         Each polynucleotide consists of monomers called nucleotides. A nucleotide is itself composed of three parts: a nitrogenous base, a pentose (five-carbon sugar), and a phosphate group. [[The portion of this unit without the phosphate group is called a nucleoside]]

ð The nitrogen bases are rings of carbon and nitrogen that come in 2 types:

1.       A pyrimidine has a six-membered ring of carbon and nitrogen atoms.

~ there are :: cytosine (C), thymine (T), and uracil (U).

2.       Purines are larger, with a six-membered ring fused to a five-membered ring.

~there are :: adenine (A) and guanine (G).

o    The specific pyrimidines and purines differ in the functional groups attached to the ring. Adenine, guanine, cytosine are found in both DNA and RNA; thymine is found only in DNA and uracil only in RNA.

ð The pentose connected to the nitrogenous base is ribose in RNA and deoxyribose in DNA. Their only difference is deoxyribose lacks an oxygen atom on the second carbon in the ring; hence its name.

o    Because the atoms in both nitrogenous base & the sugar are numbered, the sugar atoms have a prime (‘) after the number to distinguish them. Thus, the second carbon in the sugar ring is the 2’ (2 prime) carbon & the carbon that sticks up from the ring is the 5’ carbon.

-         The addition of a phosphate group to the nucleoside creates a nucleoside monophosphate or nucleotide.

-         Polynucleotides are synthesized when adjacent nucleotides are joined by covalent bonds called phosphodiester linkages that form between the –OH group on the 3’ of one nucleotide and the phosphate on the 5’ carbon of the next.

·         This creates a repeating backbone of sugar-phosphate units, with appendages consisting of the nitrogenous bases.

-         The two free ends of the polymer are distinct.

·         One end has a phosphate attached to a 5’ carbon; this is the 5’ end.

·         Another end has a hydroxyl group on a 3’ carbon; this is the 3’ end.

 

 

 

 

 

 

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-         The sequence of bases along a DNA (or mRNA) polymer is unique for each gene.

·         A gene’s meaning to the cell is encoded in its specific sequence of the 4 DNA bases

·         The linear order of bases in a gene specifies the amino acid sequence – the primary structure – of a protein, which in turn specifies that protein’s three-dimensional conformation and function in the cell.

-         An RNA molecule is a single polynucleotide chain. In contrast, DNA molecules have two polynucleotide strands that spiral around an imaginary axis to form a double helix.

(the double helix was first proposed as the structure of DNA by James Watson & Francis Crick)

-         The sugar-phosphate backbones of the 2 polynucleotides are on the outside of the helix.

·         The two backbones run in opposite 5’ => 3’ directions from each other, an arrangement referred to as antiparallel.

-         Pairs of nitrogenous bases, one from each strand, connect the polynucleotide chains with hydrogen bonds and are in the interior of the helix.

-         Most DNA molecules have thousands to millions of base pairs.

·         Because of their shapes, only some bases are compatible with each other.

ð Adenine (A) pairs with thymine (T) ,, Guanine (G) pairs with cytosine (C)

·         With these base-pairing thingy, if we know the sequence of bases on one strand, we know the sequence on the opposite strand. The two strands are complementary.

-         In preparation for cell division, each of the two strands of a DNA molecule serves as a template to order nucleotides into a new complementary strand. The result is two identical copies of the original double-stranded DNA molecule, which are then distributed to the daughter cells.

-         Genes and their products (proteins) document the hereditary background of an organism.

-         The linear sequences of nucleotides in DNA molecules are passed from parents to offspring; these sequences determine the amino acid sequences of proteins.

-         Two species that appear to be closely related based on fossil and molecular evidence should also be more similar in DNA and protein sequences than are more distantly related species.

·         For example, comparing the sequence of 146 amino acids in a hemoglobin polypeptide, humans & gorillas differ just 1 amino acid,, humans & gibbon differ in 2 amino acids ,, humans & rhesus monkeys differ in 8 amino acids.

·         More distantly (อย่างห่างไกล) related species have more differences. (ex. Humans & mice differ in 27 amino acids ,, humans & frogs differ 67 amino acids)

-         Molecular biology can be used to assess evolutionary kinship.

-         With each increasing level of order along a hierarchy of structural levels, new properties emerge in addition to those of the component parts. 


 

download link =)
http://www.mediafire.com/?mdmahi2hm0i

This review sheet is 9 pages long (with 3-4 pictures)
TT^TT i summarize from a 22-page-long chapter into 9-page-long rs 
[and i hurt my eyes a lot reading those little text in the book -_-] 

so ... just say thnxq T^T~
gdluckk 

btw i didn't proofread it at all since it is too long 5555