In homology modeling, what amino acid would you substitute threonine for if you want to test if threonine is required for catalytic activity in a protein?
Threonine can be replaced by serine (amino acid) for catalytic activity because both of them have nearly same hydropathy index.
Reason to support: Protein folding is governed by hydropathy
index of amino acid , higher the hydropathy index more it is
possible that the amino acid will reside interior of the protein
and vice versa in case of hydrophilic amino acid. So a hydrophobic
amino acid can only be replaced by hydrophobic amino
acid.
Also, threonine is hydrophilic so it can be replaced by serine
which is also a hydrophilic amino acid for the catalytic
activity.
In homology modeling, what amino acid would you substitute threonine for if you want to test...
BINF4000 chapter 7, question 6 You have a protein sequence and you want to know iis structure in a short time. you perform BLAST and PSI-BLAST searches of the PDB and you find a sequence with 15% amino acid identity to your protein. The e-value is .5. Which of the following options would you choose to achieve your goal. A. Use X-ray crystallography B. Use NMR spectroscopy C. Submit your sequence to a protein structure prediction server that performs homology...
IPP) The essential amino acid "L-Threonine" has 2 chiral carbons. It's IUPAC name is (2S, 3R) 2-amino-3-hydroxy-butryic acid" and it's structure is show below. NH 73 но,с он A) In the framework below on the left please draw a Fischer Projection for "(2S, 3R) 2-amino-3-hydro butryic acid" B) In the framework below on the right please draw the Fisher Projection for the enantiomer to your "L threonine (2S, 3R) 2-amino-3-hydroxy-butryic acid Enantiomer) Switch L-bot CH3 он tes 4 What is...
7. (6 points) Devise a synthesis to the amino acid threonine using the organic precursors from the chemical bank and any transformation we have learned in organic I and II. You will not use all of the compounds in the chemical bank. Target Chemical Bank: NaCN NH BrMg
You are given the below piece of Template DNA. What is the third amino acid in the protein encoded by this gene? 3'A ATACGGGGAGCTTTACAGAATTCAAATCAS' SECOND POSITION с A U phenyl- alanine tyrosine cysteine U U с A serine leucine stop stop stop tryptophan G histidine U с А с leucine proline arginine FIRST POSITION glutamine THIRD POSITION G isoleucine asparagine serine U с А A threonine lysine arginine methionine G U valine slanine aspartic acid glutamic acid glycine А G...
fill in the blanks
the words are
1- unfolding
primary amino acid sequence
regained
hydrogen
disulfide bond
inactivity
instructions
non covlent
lost
refolded
secondy structure
QUESTIONS 1 poi In the Anfinsen's experiment the strong and the weak bonds of the enzyme Ribonuclease A were broken using urea and a reducing agent. This lead to of the protein polypeptide chains and loss of the protein's When the chemical agents were removed, the protein and its catalytic activity. This showed that the...
10) Would an amino acid with the given side chain be most likely found in the hydrophobic or hydrophilic region of a protein? -CH-CH3 он CH2-CH-CH3 он CH3 11) What process occurs when heat, acids, bases, and heavy metal ions cause loss of biological function of a protein? 12) Answer the following questions regarding enzyme activity: a) The optimum temperature and pH for most biological enzymes is b) The molecules to which an enzyme binds are called the c) The...
While comparing the amino acid sequences of many different GPCRs, you notice the presence of conserved serine and threonine amino acids on the same cytosolic region of each receptor. You change the DNA sequence so that all of the conserved serine and threonine amino acids in the cytosolic region are converted to glutamic acid. Which of the following effects would you most likely see when cells expressing this modified GPCR are exposed to ligand compared to your control cells that...
Which sequence of amino acids, if any, would you predict to find in the interior of chymotrypsin (not the active site)? A. threonine, arginine, tyrosine B. glutamic acid, isoleucine, lysine C. valine, tryptophan, glycine D. None of the above. The answer is C, please explain why? Is it because those are hydrophobic amino acids?
What is the gene sequence(FASTA format) and amino acid sequence for the CFTR gene/protein? If you can provide a link to where you find this, that would be amazing!
Site-directed mutagenesis replaces a specific amino acid in a protein with a different amino acid, and this approach is commonly used by biochemists to determine if an amino acid is essential for a protein’s function and probe that residue’s role in that function. Which of each pair of amino acid substitutions listed below would you expect to disrupt protein structure the most? Explain. a. Gln replaced by Glu or Asn b. Lys replaced with Asp or Arg c. Thr replaced...