ENERGY vum Intermediate folding states Folded protein ww CONFIGURATION Figure 1: The Thermodynamics of Protein Unfolding²
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- The process of a protein folding from an inactive unfolded structure to theactive folded structure can be represented by the following equation: unfolded protein ⇌ folded proteinThe values of ΔH° and ΔS° for the folding of the protein lysozyme are: ΔH ° = -280 kJ/ mol ΔS ° = -790 J/mol • K(a) Calculate the value of ΔG° for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable? (c) At what temperature would the ratio of unfolded protein to foldedprotein be 1:5?The cell membrane is both fluid and asymmetrical. Discuss asymmetry of the plasma membrane, as well as the enzyme involved. Explain properties that contribute to the fluidity of the cell membrane?. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?
- Theoretical and experimental measurements show that in many cases, thecontributions of ionic and hydrogen-bonding interactions to ΔH for proteinfolding are close to zero. Provide an explanation for this result.[Low Glucose (Low Amino Acid) High Na Inside cells: THigh Glucose [High Amine Acid) Low Na) ER Nucleus Nule Blood vessel N Pump Neuoe te franperer Glucose Caer NAA Ce-apote Amine Acid Carier Secondary Primary active transport Facilitated active transport Diffusion In which direction would you expect Amino Acids to flow based on this diagram? OLumen of small intestine --> Inside small intestine cells- Blood vessel Lumen of small intestine Inside small intestine cells Blood vessel Small intestine cells -Lumen of small intestine Blood vessel Jr D00 44 20 F3 F1 F2 %23 2 3 5 7 8 * CO 241. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
- 8. For protein adsorption to the types of material surfaces designated below, indicate whether the adsorption process is primarily mediated by either enthalpic or entropic effects. Briefly justify your answers for each case. (A) A material surface functionalized with nonpolar groups (i.e., hydrophobic). (B) A material surface functionalized with polar groups (i.e., neutral hydrophilic). (C) A material surface functionalized with charged groups (i.e., +/-).III. Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow. 9.) КОНРЫ(СH-CО)» 10.) Glyoxilic Acid/Conc. H2SO4. Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to AH for protein folding are close to zero. Provide an explanation for this result.,
- Describe the tertiary (3º) structure of proteins and the different types of intermolecular forcesinvolved. Provide a structural example for each force.Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, Ion exchange chromatography is conducted via a software using DEAE-cellulose and method of elution is done by salt gradient. pH is set to 7. In terms of Molar, start of gradient is 0 and end of gradient is 1. The following graph is generated. Using the graph and analytical methods, determine pI of protein.dentify the structure labeled A (thick line) I Choose | (Choose dentify the structure labeledB Cell membrane dentify the structure labeledC Cell wall Nucleus Jentify the structure labeled D (thin line belween the whiteeand purple) yloplasm