Biochemistry
How do you identify the most conserved residues in a protein superfamily identification?
The most conserved residues in a protein are generally identified by GENOME ALIGNMENT. The computational data is obtained along with the peaks which gives the corresponding information. The peaks are observed although highly complex data is obtained these peaks shows regions of high sequence similarity showing that it is highly conserved.
Protein mass spectrometry is used to study the fragment proteins and other genomes.
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Biochemistry How do you identify the most conserved residues in a protein superfamily identification?
Biochemistry What is the protein domain in the context of a sequence alignment algorithm? How do you identify domain sin PFam?
You want to study the proximity of two residues in clamp region of a protein. Draw a schematic of your protein and label two locations of your fluorophores. Explain how your fret fluorophores would determine if these two residues were close to one another
How do you find the minimum molecular weight of a protein when given info about their residues? Protein of interest put is Resin and it is put through gel filtration. 8g of the protein are obtained and it is found to have 2 residues: isoleucine and glutamate. If analysis shows 0.124mg of isoleucine and 0.209mg of glutamate, what is Resins minimum molecular weight?
You recently joined a biochemistry research lab to study protein functions in diseases. In the lab, researchers have been working on a protein kinase, the enzyme that catalyzes the phosphoryl transfer reaction from ATP to the -OH group on serine or threonine residues of the target proteins. The researchers in the lab have found that a point mutation in the gene encoding the protein kinase leads to a change in one amino acid of the enzyme, which causes an increase...
Actin is one of the most evolutionarily conserved proteins. What does this tell you about the structure and function of this protein in eukaryotic cells?
Biochemistry Styrer Chapter 3 Problem 1. 1. Valuable reagents. The following reagents are often usedin protein chemistry: CNBr Trypsin Urea Performic acid Mercaptoethanol 6 N HCl Chymotrypsin Phenyl isothiocyanate Which one is the best suited for accomplishing each of thefollowing tasks? (a) Determination of the amino acid sequence of a small peptide. (b) Reversible denaturation of a protein devoid of disulfidebonds. Which additional reagent would you need if disulfide bonds were present? (c) Hydrolysis of peptide bonds on the carboxyl...
In Biochemistry- How do you know if you need to use the quadratic equation for weak acid problems? (Or, how do you know that the “x is small assumption” is correct?) Why does this work?
Protein Biochemistry Answer should be 1-2 A4 pages Describe how the structure of chymotrypsin enables it to cleave substrate peptides at specific locations. Use diagrams and structures to illustrate your answer.
Part B Assume a protein is composed of 115 amino acid residues and that each amino acid can have three possible orlentations How many total possible orietations are thore do he rot Express the number of possible orientations to three significant figures. ΑΣφ 345 orientations Submit Incorrect; Try Again
can you solve the following chemistry/Biochemistry
questions. thank you in Advance!
Activity: Skill Development 1. Do you think a denatured protein is biologically active? Support your answer. 2. When lemon juice is added to milk, the milk curdles. Why does lemon juice have this effect? What is happening to the proteins in the milk? 3. Some denaturation of proteins can be reversible. Which of the following denaturations do you think can be reversible? a. Heating a protein above 50 °C...