B-subunit Histidine 146 NH + H ÓH NH, Aspartate 94 H2N Which statement concerning NH2 this salt bridge is TRUE?
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- Allosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.A chain NH3 NH3 B chain Gly Phe 2. The protein pictured below is bovine insulin. Determine the number and the size of the fragments that would be generated upon treatment with the following: İle Val Val Asn Gln Gln 5 Ġln 5 His look for the cleavage points (a) without DTT and (b) with DTT. Cys Leu Cys S-S Cys Without DTT With DTT Ala Ģly Ser Ser Trypsin 10 Val 10 His Cys Leu Chymotrypsin Ser Val Leu Glu BrCN Tyr Ala 15 Gln 15 Leu Leu Тyr Ġlu Leu Ásn Val Тyr Cys 20 Çys 20 Gly Asn Glu Arg Reagent (source) Trypsin (bovine pancrease) Chymotrypsin (bovine pancrease) Staphylococcus V8 protease Pepsin (porcine pancrease) Cyanogen bromide (chemical)(CnBr) Specificity Lys, Arg (C) Phe, Trp, Tyr (C) Glu, Asp (C) Phe, Trp, Tyr (N) Met (C) Gly Phe 25 Phe Тyr Thr Pro Lys 30 Ála. 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?
- 1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. (). (a) Explain the biochemical basis for the fact that one can synchro- nize cell populations þy treating them with deoxythymidine. (b) Explain the apparent paradox that dATP at low concentrations is an activator of ribonucleotide reductase, whereas at higher concen- trations it becomes inhibitory.
- Hi - I have the following as a question in my biochemistry course and I am just lost on where to start. Thanks! Cyt cb562 will form a tetramer in the presence of Zn+2 or in the absence of Zn+2, it will form a trimer. For both the tetramer and the trimer, suggest the identity of three different amino acids that could be on the interface. Explain how your selections facilitate these interactions.о 6. What is the catalytic triad and what particular protein family would you find this? What is the general role of the catalytic triad? Predict what would happen if Asp were mutated to Gly. ructure formation of alpha heliIf you were to mutate Ser195 in the catalytic triad of chymotrypsin to another amino acid, which amino acid change would you expect to have the least effect on chymotrypsin catalytic activity? O Ala O Val O Phe O Thr O Leu
- (i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?Part C Using the values of pKas in the table below, calculate the pI for DTLH. Properties of some amino acids found in proteins Name Aspartic acid Abbreviations: 1- and 3- letter codes D, Asp Histidine H, His Leucine L, Leu Threonine T, Thr ΓΙ ΑΣΦ Submit pKa of a-COOH pKa of a-NH3+ pKa of lonizing Group Group Side Chain Express your answer to two significant figures. Request Answer 2.1 1.8 2.4 2.6 ? 9.8 9.2 9.6 10.4 3.9 6.0Which of the following statements is true O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine OLipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group
