Week 1 notes!
Week 1 notes! BIOB 260 - 00
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This 6 page Class Notes was uploaded by Ashley Alexander on Tuesday September 22, 2015. The Class Notes belongs to BIOB 260 - 00 at University of Montana taught by Scott Samuels (P), Mark Lindsay Grimes in Fall 2015. Since its upload, it has received 37 views. For similar materials see Cellular and Molecular Biology in Biological Sciences at University of Montana.
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Date Created: 09/22/15
Cell Molecular Biology 260 9215 Central Dogma Replication 9 DNA copy same language Transcription 9 DNA to RNA copying in same language but in a shorthand version Translation 9 RNA to Amino Acids change the language whole new alphabet Chemistry Concepts Appreciate the chemical nature of life Chemical bonds are used to build biomolecules Multiple weak interactions allow for complex relationships between molecules Cells are 70 water 36 organic compounds 1 Salts Bonds Covalent bonds are the sharing of electrons and arguably the most important bonds in liVing things Other bonds include Ionic Hydrogen Electrostatic dipole Vander Waals Induced Dipole Double bonds cannot rotate about each other like single bonds do Phosphate esters from to a free hydroxyl group often this is how phosphate attaches to protein chains phosphate carboxyl group high energy bond eg ATP Polarity 9 the unequal sharing of electrons due to difference in electronegativity that results in a charged molecule Stereoisomers 9 Same atoms but different arrangements often presented as a mirror image Monomeric subunits must all have the same orientation in order for their larger units to be built Most amino acids are in L form Most Sugars are in D form Hydrophobic interactions 9 hydrophobic molecules are not attracted to each other but water forces them together in order for water s molecular movements to remain uninhibited by large nonsticky molecules This concept is important to form biomembranes Electrostatic and hydrogen bond interactions are weaker in water because they are so prevalent in water and there is competition for attraction Functions of Weak Bonds Specificity 0 Enzyme Substrate o Antibody Antigen 0 Receptor Ligand signaling between cells Structure 0 Proteins 0 DNA Biomembranes Multiple Weak Interactions A lot of Velcro Why a lot of weak bonds instead of one strong one Covalent bonds take too much energy to break Cells rely on the ability to be dynamic constantly changing Phospholipid 9 Hydrophilic head Hydrophobic tail Biological molecules Subunit Chain Sugar 9 Polysaccharide Amino Acid 9 Protein Nucleotide 9 Nucleic Acid Amphipathic Molecules that possess hydrophobic and hydrophilic regions Amino Acids All are composed of a carboxyl group an amino group an R group Amino acids link together to form proteins through peptide covalent bonds Read polypeptide chain from N nitrogen terminus to C carbon terminus Cell Molec 94 Principles of Polymerization Proteins and Nucleic Acids are composed of limited monomers Information is encoded by the sequence of monomers Therefore all polymers carry information Nucleic acids are the only ones that can carry genetic information Simple sugars All sugars share a carbon backbone Each sugar has at least one hydroxyl group OH Sugars With more than 5 carbons form a ring Glycogen and cellulose are simple sugars linked by a glyosidic bond Biological Molecules Lip ds Fats energy storage long term Steroids Cholesterol bio membrane buffer structure and blood uidity o Hormones eg Testosterone amp estrogen Fatty Acids Long unbranched hydrocarbon chains With a hydroxyl group COOH at one end These molecules are hydrophobic because they are large nonpolar molecules StLOidS Fourringed hydrocarbon skeleton Phospholipid Composition Polar Head Glycerol backbone Fatty Acid Chains Micelle monolipid bilayer made from phospholipids With just one FAC Liposome bilayer ball Bilayer sheet membrane 0 A double bond in a FAC causes a bend A lipid With a double bond is unsaturated Unsaturated fat liquid at room temp Saturated fat packed tightly together Trans Fats Super bad for you stiffer than saturated fats and our body can t break them down Made rigid by too many double bonds gtkglycolipids just like a phospholipid but without the phosphate Proteins Tremendous Variety Plethora of functions Made up of linear polymers of Amino Acids 0 Principles of protein structure and function 0 FUNCTION IS DERIVED FROM STRUCTURE o N C C N C C N C C N pattern of peptide bonds 0 Different amino acids have different properties differences in hydrophobicity and hydrophilicity cause proteins to fold into specific shapes 0 Amino Acids 9 Monomeric building blocks of proteins joined by covalent bonds 0 20 standard Amino Acids they all have the same general structure 0 All organisms use the same Amino Acids o The sequence of AA determines the shape and function of a protein Amino Acid H V Carbox lGrou A 39 y p m1no H Group R R group identity group Nucleotides Nucleic Acids carry out chemical energy reactions Combine with other molecules to form coenzymes Intracellular signaling Pyrimidines Cytosine Thymine Uracil Purines Adenine Guanine Nitrogen containing rings 9 bases RiboseDeoxyribose 9 sugar group Phosphate group Base sugar Nucleoside Base sugar phosphate Nucleotide ATP Adenine Triphosphate Energy currency of the cell Breaking a phosphate releases energy Storage of genetic info Read from 5 3 carbon because the phosphate group attaches to the 5 carbon and the next nucleotide binds to the 3 carbon One less hydroxyl group than RNA in its sugar group deoxygenated Other Nucleic Acids AMP adenosine monophosphate dAMP deoxyadenosine monophosphate UDP uridine diphosphate ATP adenosinetriphosphate Summary Macromolecules 9 function determined by sequence 9 made from monomers that are slightly different from one another 9 composed through condensation reactions a molecule of water is lost With the addition of each monomer opposite of condensation reactions is hydrolysis Which breaks macromolecules down
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