Answer is : B and C only.
--Active sites have R group lining. R group help a substrate to attach to the active site or catalytic site.
-- tertiary structure of protein are the consequence of the interactions between the R are groups in their primary structure. Includes hydrophobic interactions, ionic interactions, hydrogen bonds, van Der waals interactions and disulphide Bridge formatio.
Question 3 (1 point) An amino acid's side chain (R-group) is capable of which of the...
Problem 3 Side Chains in Tertiary Structure Predict whether each of the following amino acid side chains would more likely be on the surface or in the interior of a protein after it has folded into ts tertiary structure a. tyrosine b. a. tyro sine b.leucine
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative polarity of their side chain. Consider a folded protein in an aqueous environment; where would the hydrophobic amino acids likely be found? -Tucked away in the middle of the folded protein -Randomly distributed throughout the protein -Exposed on the exterior surface of the folded protein 2. All proteins exhibit a primary, secondary, and tertiary structure, but not all proteins exhibit a quaternary structure. Describe...
17. Which of these amino acids has a thiol group as part of its side chain? a. cysteine tyrosine Aca histidine threonine e: alanine 18. Which structure correctly represents an amino acid zwitterion? C- OH. NH R CH C- OH NH, NH R- CHHC OH NH NH
Lumpur QUESTION 2 Myoglobin is a globular protein. About half of its 153 amino acids have nonpolar side chains. Where would you expect those amino acids to be located in the tertiary structure? Inside the compact tertiary structure Outside the compact tertiary structure Evenly distrubuted On the edges of the amino acids primary chain QUESTION 3 What type of bonding is responsible for the primary structure of a protein? covalent bonds hydrogen bonds ionic bonds alpha helices
26. Which of the following classification does not match the amino acid side chain A) Contains an basic group/ lysine B) It is polar C) Forms disulfide bond/ cysteine D) Forms hydrogen bonds with neighbors/ alanine serine 27. All amino acids found in proteins are L-amino acids EXCEPT the achiral. A) glutamate B) Lysine C) glyeine D) Alamine 28. The plH at which the positive and negative charges of an amino acid balance each ofher is called the A) isotonic...
Question 30 (1 point) Saved If an amino acid with a nonionizable side chain has a pka for its a-carboxyl group of 2.4 and a pka for its a-amino group of 9.8, what is its pl? 12.2 Not enough information 06.1 07.4
The pK of the side chain of amino acid X in a polypeptide is normally in the range of 9-10 and carries a positive charge when protonated. Suppose you have a soluble globular protein and you find there is an X that has a pK of 6.5. What is the most likely reason for such a large drop in pK? Circle the correct answer. a) X is on the surface of the protein where it ion pairs with the carboxylate...
20. In most proteins this amino acid's side chain is found
clustered away from the aqueous exterior of the protein as a result
of which interaction?
a) Hydrophobic effect
b) Charge-charge (ionic)
c) Dipole-dipole
d) Van der Waals (dispersion)
A protein has a pI of 6.5. If I want to use an anion exchange
resin (there is a +ve charge on the resin) to bind the protein,
what pH could I perform the separation at?
a) pH 8
b) pH...
What is the classification of the side chain R group in the amino acid shown here? HN CH-C-0 CH-CO A) acidic CH B) basic C) neutral
What is the classification of the side chain R group in the amino acid shown here? O A) acidic HN-CH-C-0 CH2 B) basic HN C) neutral -NH