I need the answer as soon as possible A Leu-Ala mutation at a site buried in the core of the enzyme lysozyme is found to be destabilizing. Explain the observed effect of this mutation on lysozyme stability by predicting how enthalpy (AH), conformational entropy(ASpeptide), and the hydrophobic effect (ASsolvent) are expected to change for the mutant compared to wild-type lysozyme. Explain how AG for unfolding is affected by your predicted changes in enthalpy or entropy.Match the items in the left column to the appropriate blanks in the sentences on the right.Reset HelpAS polvent F-¬U (WT)1. Due to loss of van der Waals Interactions in the folded state,willhydrogen bondsbe more thanlarger2. ASgolvent is likely to beunfavorable for the mutant because theclathrate structure insmallerAla side chain is predicted to haveWTthe unfolded state than the WT Leu side chain. Thus,will be less thanthe mutantAHF-U (WT)3. These entropic and enthalpic effects make AGF-U more unfavorable for(i.e., theis more stable to unfoldingvs.van der Waals interactionsthanAHr-U (mut)ASprotein4.because differences in conformational entropy around o (Phi) and(Psi) angles arefor Leu vs. Ala.ASprotein F-+U (WT) > AS protein FU (mut)AS solvent F-U (mut)5. Thus, the differences in AH andboth predict that the mutant will bestable to denaturation than the WT protein.moreASprotein F-U (WT) < ASprotein F-U (mut)lessAS protein F-U (WT)z ASprotein F-U (mut)ASsolvent

The Leu to Ala mutation in the buried core of the protein lysozyme causes a destabilization in the…

Match the items in the left column to the appropriate blanks in the sentences on the right. Reset Help ASlvent F-U (WT) 1. Due to loss of van der Waals interactions in the folded state, will hydrogen bonds be more than larger 2. ASpolvent is likely to be unfavorable for the mutant because the smaller Ala side chain is predicted to have clathrate structure in WT the unfolded state than the WT Leu side chain. Thus, will be less than the mutant

Match the items in the left column to the appropriate blanks in the sentences on the right. Reset Help ASlvent F-U (WT) 1. Due to loss of van der Waals interactions in the folded state, will hydrogen bonds be more than larger 2. ASpolvent is likely to be unfavorable for the mutant because the smaller Ala side chain is predicted to have clathrate structure in WT the unfolded state than the WT Leu side chain. Thus, will be less than the mutant

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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