removed aher the reducing agent was removed? a. The protein would not fully unfoid lidenaturel. participste in weak bonding interactions with RNane, preventing oxldation of Cys C. Disulfide bonds are not positioned correctly unless weak bonding Inberactions are present d the completely unfolded enayme, with all-5-5-bonds broken, is still enrymatically active wauid form e the RNase preparation covalent bonds with 25. which ligand binds tightest? a Igand A, with a K 10 M h. lgand 8, with aKa 10M .gand C, with a percent occupancy of30% at 1PM d·ligand D, with a percent occupancy of 80% at 10nM 26. What is ehe nature of the mutated amine acd nemgbin that causes sidkile cell divease? a. It lis a mutation from an acidic to a basic residue that ereates a new salt bridge and leads to hemoglabin fibril formas b. it is a mutation of histidine to alanine that disupts heme binding, completely abolishing oygen binding. c is a mutation from an acidic to a hydrophobic residue that creates a hydraphobic patch and leads to hemoglobin f formation theough hydrophobic interactions binding of oxygen. folding and becoming functional 27. The enaymatically catalyned reaction shown below is an example of d.tis a mutation from an acidetoahrdrophobic residue that erupts tenrainer form⦠and thustho cooperative a mutation from a hydrophobic to an acidic residue inside the protein core that prevents hemogiobin from prep e. hydrolase 28 What is one effect produced by an enuyme on the general reaction below? ion is lowered. reactonquilib The concentration of the reactants is increased The formation of the transition state is blocked. æ "roonwlease has·tumover number per second of 100, how many molecules of RNA can one melecule of rito nudea in 25 minvtes 150 d.150,000 e.900,000 30. Calrulate the K 25 mM. for an enryme that has a V of 12 mM/s and has shown to have a Vo of 4 mM/s at a substrate con forces that lead to the folding of a globular protein in aquera