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Biochemistry Homework Help | Biochemistry Assignment Help

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Biochemistry Topics & Concepts Covered

TOPICS	CONCEPTS
Biomolecules	Proteins, Nucleic Acids, Lipids, Carbohydrates
Enzymes	Enzyme Kinetics, Inhibition, Catalysis
Metabolism	Glycolysis, TCA Cycle, Oxidative Phosphorylation
Molecular Genetics	DNA Replication, Transcription, Translation
Cell Signaling	Signal Transduction Pathways, Cellular Communication
Biochemical Pathways	Biosynthesis of Macromolecules, Metabolic Pathways
Protein Structure & Function	Primary, Secondary, Tertiary, Quaternary Structure
Enzyme Mechanisms	Active Sites, Substrate Binding, Catalytic Reactions
Bioenergetics	ATP, Thermodynamics, Energy Conversion
Carbohydrate Metabolism	Glycogenesis, Glycogenolysis, Gluconeogenesis
Lipid Metabolism	Fatty Acid Synthesis, β-Oxidation, Lipid Signaling
Amino Acid Metabolism	Amino Acid Catabolism, Biosynthesis, Urea Cycle
DNA Replication & Repair	DNA Polymerases, Proofreading, Mismatch Repair
RNA Transcription & Processing	Promoters, RNA Splicing, Ribosome Biogenesis
Protein Synthesis	Translation Initiation, Elongation, Termination
Cell Cycle & Division	Cell Cycle Phases, Cell Cycle Regulation
Hormones & Signaling Peptides	Endocrine Signaling, Hormone Classes, Signal Cascade
Membrane Structure & Function	Fluid Mosaic Model, Transport Mechanisms
Enzyme Regulation	Allosteric Regulation, Covalent Modification
Biochemical Techniques	Spectroscopy, Chromatography, Electrophoresis

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Recently Asked Biochemistry Questions

Expert help when you need it

Q1: Explain the role of eicosanoids formed as a result of metabolism of n-3and n-6 fatty acids in human physiological processes. In your answer consider data from relevant observational (epidemiological) studies alongside explanation of mechanism of action of these eicosanoids.2.See Answer
Q2: Evaluate the evidence for the effect of fibre on satiety. Translate the evidence behind using dietary fibre to regulate satiety into practical advice that you would give to someone wishing to lose weight. Use appropriate information from research literature.3. In your answer consider data from relevant observational(epidemiological) studies alongside explanation of mechanisms of action of dietary fibre on satiety.(25 marks)See Answer
Q3:Discuss the clinical presentation of this case & relate it to the laboratory findings and interpretations. See Answer
Q4:Discuss all abnormal results and explain the underlying cause/s of each abnormal laboratory result. See Answer
Q5:Describe the acid-base disturbance and explain WHY you have reached this condition. See Answer
Q6:Calculate the anion gap and comment on its significance. Describe what could be the cause of the abnormality, if applicable. See Answer
Q7:Calculate the plasma osmolality and comment on its significance. See Answer
Q8:Explain which result/s are most indicative of diabetes condition. See Answer
Q9:What is C-peptide? Is this patient’s C-peptide concentration likely to be low, normal or high/why? See Answer
Q10:Explain the pathophysiology of the different types of Diabetes Mellitus. See Answer
Q11:Consider the enzyme-catalyzed reaction AB. You determine experimentally that the maximal initial velocity. Vmax for the amount of enzyme you have added is 50 mM of B appearing per minute. You also determine that the Michaelis constant, K. for this enzyme is 20 mM of A. What concentration of A will give an initial velocity of 25 mM of B appearing per minute?See Answer
Q12:This is a titration curve for which amino acid?See Answer
Q13:a) Briefly describe the overall tertiary structure of MHETase. (Approach this as in Problem 1.) How many and what kind of domains does the polypeptide have (e.g., what class)? Even if you think that there is a single domain, would there be a way to divide it into 2 sub-domains? Specify which parts of the polypeptide below to each domain or sub- domain (unless you think that there is only 1 domain and no sub-domains).See Answer
Q14:b) MHETase is believed to use a catalytic triad to hydrolyze the ester linkage in MHET, just like the catalytic triad in the serine proteases. Examine the structure of MHETase complexed with the analog and identify the 3 residues in the catalytic triad. For each one, find the most important distance between that residue and its partner in the mechanism and fill out the chart, identifying the 2 atoms used and the distance between them. Also identify the secondary structure in which it is found (e.g., a-helix, ß-strand, tight turn, or loop). Residue (name & #) Ser His Asp Identify the most relevant inter-atomic distance and identify the atom name (click on it in PyMOL) (e.g., "CB" or "C4" or "OG") Atom in Ser: Atom in substrate analog: Atom in His: Atom in Ser: Atom in Asp: Atom in His: distance between atoms (Å) 2° structural context/nWhat other residues in the enzyme are important for binding MHET? Identify at least 4 that seem to play an important role. Residue (chain, name & #) Atom of the residue and the substrate analog? distance Type(s) of interaction (e.g., H-bond, between charge-charge, coordination bond, van der Waals) atoms (Å) 2⁰ structural context Which, if any, of these residues might explain why MHET is a good substrate, but BHET is not? And how would it explain the substrate specificity?See Answer
Q15:c) The enzyme contains 5 disulfide bonds. Given that this is a secreted enzyme, is this expected or surprising? List the 5 disulfide bonds below (e.g., "Cys41 - Cys142") and circle the one that you would expect to be most important for enzyme activity.See Answer
Q16:d) Going back to the first question, briefly discuss the roles of the 2 (sub)domains in the mechanism of MHET hydrolysis. Broadly speaking, what role does each one play?See Answer
Q17:Consider the reaction mechanism shown below for this question: CH₂ CH₂ NH₂ CH₂ CH₂ Lyase O Ligase 6 Oxidoreductase Transferase O Hydrolase CH₂₂ CH₂ 0,PO 5 CH CH₂ What class of enzyme does this belong to? O Translocase CH₂ 20,P H₂C CH₂ CH₂ 2 CH₂ 20,PO CH₂ 20,PO Net₂See Answer
Q18:Bonus: Determine the primary sequence of the following peptide. (10 Pts) A. Trypsin treatment generated the following fragments: (LFVCYMGFR) (HDITNAATYR) (AEK) (CPS) (K) (QIVAAR) (LWVANK) B. Chymotrypsin treatment generated the following fragments: (AEKL) (F) (VCY) (MGF) (RHDITNAATY) (RL) (W) (VANKKQIVAARCPS) C. Thermolysin treatment generated the following fragments: (LF) (VCY) (MGFRHD) (ITNAATYR) (AEK) (LW) (VANKKQ) (1) (V) (AARCPS) Legend: Trypsin = Lys & Arginine (R.) Chymotrypsin = Tyr, Trp, Phe, Leu (R.) Thermolysin = Leu, Val, lle, Met (R₂)See Answer
Q19:1. Why does EDTA (structure shown below) quench DNA polymerization reactions at physiological pH? Show the mechanism involving the atoms in EDTA that may be responsible (3 points) میری HO HO OH OHSee Answer
Q20:2. A DNA polymerase is isolated and found to have an error rate of 1 in 106. (6 points, 3 each) A. Suppose that the error rate is determined solely by the relative stabilities of incorrect and correct base pairs. What would the difference in free energy between correct and incorrect nucleotides incorporated by the polymerase have to be in order to explain the error rate? B. Solution studies of isolated oligonucleotides indicate that the energetic difference is actually -1.2 kJ.mol-1. What is the equilibrium constant of correct-incorrect base pair discrimination based on these solution studies?See Answer

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