ChemistryA. if a protein had two aspartic acid R groups interacting at pH 2, what kind of interaction would you see in its tertiary structure? B. draw the tripeptide Gly-His-Glu at pH 7. groups.A. If a protein has two aspartic acid R.interacting at PH₂, what kind of interactionwouldyou see in its tertiaryStructureB. Draw the tripeptide Gly-His-Glu at PH 7

Since you have asked multiple question, we will solve the first question for you. If you want any…

Answered: A. if a protein had two aspartic acid R…

A. if a protein had two aspartic acid R groups interacting at pH 2, what kind of interaction would you see in its tertiary structure?

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

See similar textbooks

Related questions

Q: Draw the structure of glycine. Draw the structure of valine. Now draw them as a dipeptide

Q: Draw the structures of the amino acids formed at physiological pH when the tripeptide below is…

Q: Which statement is true Select one: O a. In earth, amino acids present in D form O b. Sugars present…

A: Biomolecules are the organic molecules present in loving organisms and very useful for the life of…

Q: ◆ Arginine Phenylalanine ◆ Cysteine ◆ Serine Glutamic acid ◆ Glutamine ◆ Isoleucine Leucine A.…

A: There are 20 naturally occurring amino acids. In a polypeptide chain, the alpha amino and the alpha…

Q: Creating tertiary structures of proteins involves the linking of amino acid functional groups with…

A: Proteins are the building blocks of the body. All the life forms consist of proteins in their cell…

Q: Protein secondary structure pricipally arises from A H-bonding of backbone atoms in peptide groups…

Q: BIOCHEMISTRY Why does adding a solution of HCl denature proteins (identify affected functional…

A: Due to its acidic nature, HCl (hydrochloric acid) can denature proteins when introduced to a…

Q: Draw out the basic amino acid structure (not specific) What is a peptide bond?

A: Proteins Proteins are macromolecules that are made up of long chains of amino acids. They are…

Q: Only 0.1% of peptide bonds have the cis configuration. Calculate the difference in energy between a…

A: A peptide bond is formed between the alpha carboxyl group of the amino acid residue at the N…

Q: Comment on why the feature ~210 nm in Circular Dichroism and Infrared spectroscopy is useful for…

A: Circular dichroism spectroscopy (CD) is a fundamental insightful method used to investigate…

Q: A protein has an isoelectric point of 7 and you have two choices of resins. One is BioRex -70,…

A: Ion exchange chromatography is a type of column chromatography, for the separation and purification…

Q: is a version of an amide bond

A: Proteins can function as structural elements (hair, wool, collagen), enzymes, hormones, hereditary…

Q: peptide bond Primary Structure Secondary Structure Tertiary Structure NH3+ Quatern Structur 2. Using…

A: Amino acids sequences linked together by peptide bonds form the primary structure of a protein. Any…

Q: BIOCHEMISTRY If the protein is more hydrophobic, then adding additional charge is not the best…

A: Several excipients can disrupt hydrophobic interactions in hydrophobic proteins without adding NaCl.…

Q: Need help by understanding what linkages would we find in the polysaccharides based on the types of…

A: The polysaccharides are joint by glycosidic linkage. But the type of glycosidic linkage is different…

Q: the steroid nucleys. (It is OK if your structure is thed somewhat It's easiest to use the…

A: Steroids play a very important role inside the body cells as a regulator of membrane fluidity. This…

Q: The aromatic side chain of Trp residues in proteins and peptides can be chemically modified by two…

A: Amino acids are classified as acidic, basic, hydrophobic and polar neutral based on the nature of…

Question

Chemistry

A. if a protein had two aspartic acid R groups interacting at pH 2, what kind of interaction would you see in its tertiary structure?

B. draw the tripeptide Gly-His-Glu at pH 7.

groups.
A. If a protein has two aspartic acid R.
interacting at PH₂, what kind of interaction
would
you see in its tertiary
Structure
B. Draw the tripeptide Gly-His-Glu at PH 7

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps with 2 images

SEE SOLUTION Check out a sample Q&A here

Similar questions

a. What is a heterocyclic amine? What was the most interesting example you found out about? Why was it interesting? b. DNA and RNA are heterocyclic amines with Nitrogen in the center. If sulfur were in the middle of the ring instead of Nitrogen how would this affect the ability to H-bond? c. Show the structure of 2 neurotransmitters. What are some of the interactions you found out about it.
ans. part d and e
Chemistry help
PART A. Redraw the table below on the whiteboard. Use your Biological Molecules Part 2 handout to fill in the missing information in Column B and C. A) Polymer Lipid DNA B) Monomer (or component units in the case of lipids). Draw the specific structure and put the name of the molecule under the structure. Fatty acids (pick 1), glycerol, glycerophospholipid Deoxynucleotide monophosphates (Pick one purine and one pyrimidine) C) Additional tasks Is your fatty acid saturated or unsaturated? How do you know? On your glycerophospholipid, identify the glycerol group, the fatty acids, and the phosphocholine. Label the hydrophilic head and hydrophobic tail. Label which is the purine and which is the pyrimidine. Circle the sugar on each.
Can you please explain how to solve this problem?
Consider the tripeptide serylalanylleucine. Part: 0 / 2 Part 1 of 2 Draw the structure of this tripeptide at physiological pH. Click and drag to start drawing a structure.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Currently working on protein structures and am having difficulty understanding the principles behind this question. [Consider the peptide sequence Ile−Leu−Trp−Ala−Asn−Arg−Met−Ser−His−Val−Leu−Phe−Ala−Val−Glu−AlaIle−Leu−Trp−Ala−Asn−Arg−Met−Ser−His−Val−Leu−Phe−Ala−Val−Glu−Ala Which amino acid residues would you expect to be on the solvent‑exposed surface once it folds into its native conformation?] What exactly am I supposed to be looking for in the structures of the amino acids?
Suppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5
Match amino Acid R group characteristics to the biochemical bond it can form. Alanine ◆ Glycine Proline Aspartic Acid Lysine Tryptophan ◆ Methionine Threonine Asparagine Histidine A. Pi-bonding aromatic bonds B. Non-polar, contains a sulfur atom C. Non polar bonds D. Amide group bonds E. Inserts a kink (non-freely rotating bond F. Anionic group donating bonds G. Hydroxy group bonding H. Cationic group with pK = 6.0 I. No-R group - highly flexible J. Cationic group donating bond
Uhhh