7. Why proteins prefer to have a-helices or ẞ-sheets in their interior core, instead of random coil loops?

The preference for alpha helices and beta sheets in the interior core of proteins is driven by a…

Answered: 7. Why proteins prefer to have…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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4. Why would a tetra peptide e.g. H-Gly-His-Gly-His-NH2 accumulate in the lysosome in a biological cell? Is it related to the acidic pH of the lysosome?
3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
17. How would you computationally predict the thermodynamic stability of a long, extended RNA helix? Please explain in 1 sentence how structural "favorability" can be predicted
How many Alpha helices and beta sheets are in ESR1? What's the percentage of alpha helices and the beta sheets?
4.) If a mutation in an organisms DNA causes the resulting protein to possess an alanine residue to be in the 13th position instead of a glycine, what level(s) of the resulting protein's structure would likely be affected? Why? Why would the other(s) not be affected? 14:
What is it about alpha helices and beta sheets that would make the coils less flexible?
6. In RNA, why can uracil be used in place of thymine? * The structural difference between thymine and uracil does not affect hydrogen bonding to adenine Thymine and uracil are actually identical bases, but they're named differently because one is in DNA and the other is in RNA Uracil forms two hydrogen bonds with adenine, but using different atoms than thymine O Uracil can interact with adenine via three hydrogen bonds 7. At least how many different types of RNA are there in eukaryotic cells? * 1: just messenger RNA 2: messenger RNA and ribosomal RNA 3: messenger RNA, ribosomal RNA, and transfer RNA 6: the three listed above in C, plus microRNA, small interfering RNA, and small nuclear RNA 1
9. Identify the N-terminal and C-terminal amino acid in each peptide. H,N-CH-C-Ņ–CH-C-o- CH2 H CH3 ČH(CH3)2 HÑ-CH-C-Ņ-CH-C-N–CH–C-O- CH2 H ČH3 H ČH,CH,CONH, a.
1)If we were to begin with protein that is 145 residues long, How many (ATP/GTP) would have to be used? (ATP hydrolysis from 1 pyrophosphate= 2 ATP)' 2)What is the corresponding codon of an anticodon GUA (ignoring the wobble).

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