Lipids, Carbohydrates, Nucleic Acids & Proteins - PDF

3 Lipids Carbohydrates Macromolecules large molecules formed bysmaller molecule linked together proteins nucleic acids carbohydrates lipids are polymers not lipials created through linkage of monomers D re...

3 Lipids Carbohydrates Macromolecules large molecules formed bysmaller molecule linked together proteins nucleic acids carbohydrates lipids are polymers not lipials created through linkage of monomers D reactions involving water form Treakapartpolymers Condensation removal of water creates covalent bond between monomers O OH H G OH Id H2o Hydrolysis addition of dimer it 0 0 0 water breaks up a covalent bond between monomers trimer H2O Lipids are hydrocarbons O O dimer C H insoluble in water be of nonpolar H2o covalent bonds when close together held together der Waals interactions by van Lipids store energy in C C C H bonds Efrelythfcivephb.ie structural role in cell membranes can serve as thermal insulation Triglycerides simple lipids have little Fats solid af room temp very polarity extremely E s.li uatouebngmrnyateenP hydrophobic consist of acids 3 fatty nonpolar hydrocarbon chain attached to a polar carboxyl group E5 Id one glycerol an alcohol w 3 hydroxyl OH groups synthesis of a triglyceride needs three condensation reaction 3140 taken T.hn fT outto bond acidsto fatty If 0 1 d o egg glycerol I 91 3 fattyacid ODD 000 acid chains can vary in length a structure  y amphipatice hydrophilic end a hydrophobic tail in saturated fatty acids all bonds between carbon atoms are IE ht i unsaturated fatty acids hydrocarbon chains contain one or more double bonds Linoleic Palmitic d Emp cause kinks in chain 00 unsatured 00 00 5 9 00 88 saturated 800 is 80 Phospholipid two fatty acids 00888g 8 00 a phosphate bound to glycerol the phosphate group has a phospholipid neg chorsetmaking the head hydrophilic Ectroph choline head phosphate Phospholipid bilayer forms from phospholipids in an aqueous enviro slyard enter P l 4ᵗʰ hydrophilic heads on outside to a 11 1 interfagogggtryhydrophilic BSSSSS bEic 888888 88 3 2 Carbohydrates polysaccharides Biological roles of carbohydrates source of stored energy transport stored energy w in complex organisms structural molecules that give shape to man organisms recognition signaling molecules that or can trigger specific biological responses cellulose used as supper structure Similiar compositions Cn H2O n stamint chaffar some carbs are smalt called simple sugars carbs polymers of the simple sugars some are lager are simple sugars 12 or fewer carbons Monosaccharides 5 or 6 carbons usually in ringpentoses hexoses Tolymersstructure dependent on the isomers of the simple sugars Disaccharides two monosaccharides linked by a glycosidic bone 11 1 d glucose t.la Haiti 20 t.to sucrose Entensation Oligosaccharides 3 10 monosaccharides joined by glycosidic  y bonds have additional functional groups many often bonded to proteins lipids on all surfaces serve as recognition signals Polysaccharides large polymers of monosaccharides Farcheffam of polysaccharides of glucose difftisangphal linkage slycosen kishkhmaged polymer of glucose main energy storage indear cellulose most abundant carbon containing organic biological compound on earth stable soodstructure 3 3 Nucleic Acids Proteins Nucleic acids are polymers specialized for storage transmisso use of genetic info DNA deoxy ribonucleic acid RNA ribonucleic acid turasterner a pentose Nantaing monomers are nucleotides base phosphate group nucleoside s Basso ee Es Bases primidines single rings 1 single purines double rings  F double Sugars W DNA deoxyribose it one pentose RNA ribose image unstable Infuse nucleotides bond in condensation reactions to form phosphodiesterlinkages 5 carbon 3 carbon of two ribose link to create sugar phosphate backbown nucleic acids 0 grow 3 0 in 5 to of direction 0 provide energy forreaction 20 monomers include small  g RNA molecule for DNA rep gene expression DNA RNA or polynucleotides long polymers RNA normally a single strand DNA normally clouble stranded held together base H bonds by complementary pairing using adenine thymine Hot asanas cytosine guanine Crb 3bonds in RNA adenine uracil A 4 sugar two strands form a ladder phosphate 59 that twists into double helix LTt all the H bonds become base strong be so many RNA folds back onto self to form short double strand regions determined base pairing structure depends folding by so on order of the bases shape of RNA affects how it  interacts w other molecules DNA info encoded in the sequence of bases Replication DNA copied into a new identical DNA molecule to be transmitted to daughter cells offspring Transcription info encoded in DNA base sequences used to make RNA Translation info in RNA base sequence used to make proteins replication DNI R polypeptide reverse transcription Genes DNA sequences that encode specific proteins are transcribed into RNA 3 4 proteins protein structure Proteins are polymers made up of Amino acids two functional Ligands groups amino group 1042 43100 Erban 20040 amigup certgdp Cooh  1 R group or side chain differ in each are grouped properties of side chain 220 common AA by proteins have enormous structural diversit amino acids linked in condensation reactions to form peptide bonds polymerization occurs in the amino to carboxyl direction cysteine side chains can w EEE Esent Bit chains this type of S S bond called a disulfide bridge or a disulfide bond Amino acid groups A elec charged hydrophilic side chains pos NH neg coolt O O O chains hydrophilic 13 polar but uncharged side OH O O O 0 0 c special cases breaks α helixes d nonpolar hydrophobic C H bonds 0 o o at end g Structure amino primary structure sequence of acid monomers in polypeptide held by peptide bonds covalent secondary structure folding of polypeptide into repeated patterns alpha helix right handed coil 0 beta pleated sheet R groups extend outfrom surface of helix notres for stabalizing helix held together H bonds by structure final folded polypeptide into tertiary a functional protein  variety of bonds forces between R groups polypeptide backbone covalent bonds disulfide bridge It bond ionic van der waals Quaternary structure two or more polypeptide chains bind together interact Denaturing beat or chemicals disrupt weak interactions secondary structure tertiary could possibly return back to normal when coded 3.5 protein function determined by binding characteristics AA side chains Ligand molecule or ion that binds to another molecule specific involve many weak bonds together a strongish interaction conformational change this binding causes a change in shape which affects the function can result in protein becoming active or inactive changing R group can also affect shape Proteolysis can remove a ligand binding or create a site for other proteins binding Some proteins need a cofactor non protein or ion to function become substrate active ex ATP vitamins offfactor active protein Enzymes lower activation energy to substrates creates which is binding freeenergy used to change shape of or break enzyme bands doesn't change amount of free energy enzymes very specific each one catalye only one chem reaction Induced fit enzyme changing shape after bonding to substrate to make tighter binding enzyme substrate complex held together through It bonds ionic bonds van der waals interactions Catabolic pathways break down molecules into smaller molecules release energy Anabolic pathways synthesize complex molecules from simplier ones  Inhibators bind to active site to prevent substrate from attaching Irreversible inhibition can occur w certain drugs rare Competitive inhibition reversible compete w substrate to attach Allosteric regulation non substrate binds to a site which changes enzyme shape now og substrate can't link affects activity can activate or inactivate enzymes Phosphorylation phosphate group added by a protein kinase in hydrophobic region incluce a change to interact w hydrophilic regions Protein Phosphates remove phosphate groupsfroms proteins help cell regulation