Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Is there a reason why you divided the pKa's by 2 when determining the pI?
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Is there a reason why you divided the pKa's by 2 when determining the pI?
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- Identify and encircle the peptide bonds in this polypeptide (Ala-Leu-Glu-Ala-Asn-Asp-Arg-Ala)?arrow_forwardIn the following polypeptide, which amino acid would be participating in hydrogen bonding with alanine, given this sequence forms an alpha helix? Please write out the full amino acid name, not the abbreviation. Met-Ala-Leu-Glu-Lys-Thr-Leu-Valarrow_forwardс" CH2 CH2 "НaN H с. CH С" CH Нзс CHз ZI о-оarrow_forward
- Translate the following amino acid sequence into one-letter code: Glu-Leu-Val-Ile-Ser-IleSer-Leu-IleVal-Ile-Asn-Gly-Ile-Asn-Leu-Ala-SerValGlu-Gly-Ala-Serarrow_forward1. Amino Acid 1 = W + X = 1 Draw amino acid 1 at a low pH a) As the D Fisher Projection Name of amino acid 1: b) As the S isomer: Argininearrow_forward4. 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.…arrow_forward
- The primary structure of b-endorphin, a peptide containing 31 amino acids synthesized by the body to control pain, is shown here: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr- Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu What fragments are obtained as a result of treatment with trypsin?arrow_forwardGive the name of the polypeptidearrow_forwardIdentify the amino acid: pic 2.png Tryptophan Asparagine Histidine Prolinearrow_forward
- +H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.arrow_forward1)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).arrow_forward8.ldentify each of the amino acid in the polypeptide and then name it using the 3-letter abbreviations. H2N- CH- CH- CH CH- CH- OH CH2 CH2 CH-OH CH2 CH2 CH2 Cн CH2 CH2 NH NH ENH NH2arrow_forward
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