BCHM 3050 1st Edition Exam 1 Study Guide Lectures 1 10 Lecture 1 January 7 The Effects of Biomolecules What are the five major functional groups that make up the biomolecules such as nucleic acids amino acids and monosaccharaides Specifically which of these function groups are in the each of the three biomolecules mentioned above Five major functional groups OH Hydroxyl NH2 Amino COOH carboxylic acid CO carbonyl POOH Phosphate group Nucleic acids contain hydroxyl amino carbonyl phosphate groups Amino acids contain amino group and carboxylic acid Monosaccharaides contain hydroxyl and carbonyl groups Lecture 2 January 9 The Properties and Importance of Water Why is water considered the ideal biological solvent Name five different properties that give water this important role 1 2 3 4 5 Partial negative of water attracts other positive ions and partial positive of water attracts other negative ions Dissociation of solute ions are surrounded by molecules CH4 is hydrophobic because it doesn t normally have partial charges on its atoms but water can still be used to dissolve it Cohesion water molecules remain together because of strong hydrogen bonds Adhesion water interacts with other surfaces plays role in capillary action of plants Surface Tension i allows some organisms to be able to walk on water ii Based on hydrogen bonding of water iii Tension of the surface of the water body iv One molecule of water participates in hydrogen bonding with four other molecules v Force exerted by the molecules at the surface is weaker vi The pull downwards is stronger than the pull upwards Lecture 3 January 12 Molarity Osmotic Pressure and pH Calculations What is the formula for molarity Molarity M moles liter What is the formula for osmotic pressure Osmotic pressure iMRT is the osmotic pressure in atm i van t Hoff factor of the solute M molar concentration in mol L R universal gas constant 0 08206 L atm mol K T absolute temperature in K 273 15 temp in Celcius How is pH used to measure hydrogen ion concentration pH log H pH pOH 14 Lecture 4 January 14 Acids Bases and Buffers What is the difference between a weak acid and a strong acid Weak acids dissociate but not completely while strong acids dissociate completely What two components make up the ideal buffer Equal concentrations of a weak acid and its conjugate base What is the Henderson Hasselbalch Equation pH pKa log A HA Lecture 5 January 16 How to Find Isoelectric Points How do you find the pI Isoelectric Point of acidic amino acids pI of acidic amino acid average the pK of the 2 carboxylic acid group DO NOT take into account the pK of the amino group How do you find the pI for basic amino acids For Basic amino acids pI pK 2 pK 3 2 Ignore the pK 1 value Lecture 6 January 21 Amino Acids and Non Standard Amino Acids What is the difference between an essential amino acid and an non essential amino acid Essential necessary in our diet but our body doesn t make them so we must ingest them Non essential synthesized by the body as break down products How many non standard amino acids are there Why are they considered non standard There are about 300 non standard amino acids Most are non protein amino acids Many are modifications of the standard amino acids A few are found in proteins All have special biological functions Lecture 7 January 23 Protein Structure and Torsion Angles Describe the difference between primary structure secondary structure and tertiary structure of proteins Primary structure specific amino acid sequence of the protein Secondary structure alpha helix or beta pleated sheet beta alpha beta is also an example of a supersecondary structure Tertiary structure group of secondary structures formed by R group interactions stabilized by hydrophobic interactions electrostatic interactions hydrogen bonds and covalent bonds What are the three different types of torsion angles that determine how the protein will look in the end Phi refers to the bond rotation between the alpha carbon and the nitrogen Psi bond rotation between alpha carbon and carbon 1 Omega bond contortion between carbon 1 and other nitrogen Lecture 8 January 26 Protein Folding and Molecular Chaperones Describe the steps involved in protein folding Protein folding cannot occur on its own requires a lot of energy from the body It starts with ribosomes translating Hsp70 attacks the protein initiates the process of protein with ATP ATP energy currency of the body more ATP molecules means more energy to store ATP is broken down into ADP releasing energy to fold the protein Folded protein handed over to Hsp60 complex GroEL barrel enzymes assist 7 molecules of ATP are broken down and GroES is added and the lid of the barrel is shut Folding occurs organic phosphates are released Lid comes off and the folded protein in released What is the role of molecular chaperones What does heat shock proteins refer to Chaperones surround guide the proteins and help them to fold Heat is one form of stress that our body is exposed to easily chaperones are trained to resist this temp heat shock proteins Most chaperones are heat shock proteins Lecture 9 January 28 Fibrous vs Globular Proteins What are the different functions of fibrous and globular proteins Fibrous proteins function as structural support systems while globular proteins function as transport mechanisms How does the oxygen affinity of hemoglobin and myoglobin differ Why does this happen Hemoglobin has a lower affinity to oxygen because it has more oxygen binding sites than myoglobin This allows for the hemoglobin to release the oxygen to the myoglobin in the tissues On the other hand the affinity for oxygen is much higher in myoglobin due to the fact that it has only one oxygen binding site Lecture 10 January 30 The Function of Enzymes What is an enzyme It is a biological catalyst that functions to speed up the rate of a biological reaction but is not altered or consumed in the reaction Enzymes are usually proteins but not always What is the difference between a substrate and a product What an active site Substrates are the substances that enzyme act on also known as reactants On the other hand products are the substances produced by chemical modification of the substrate The active site is the specific region on an enzyme where substrates bind and where the catalytic reaction occurs
View Full Document
Unlocking...