Table of Contents
- 1 What is the average molecular weight of an amino acid?
- 2 What are the factors that denature proteins?
- 3 Why would it be useful to determine the molecular weight of a protein?
- 4 Why is the molecular weight of a protein important?
- 5 Why is weight average molecular weight greater than number average?
- 6 How is the molecular weight of a protein determined?
- 7 What is the size of a tetramer with 288 amino acids?
- 8 What is the molecular weight of an inactive tetramer of in?
What is the average molecular weight of an amino acid?
110Da
The average molecular weight of an amino acid is 110Da. Dalton (Da) is an alternate name for the atomic mass unit, and kilodalton (kDa) is 1,000 daltons.
What are the factors that denature proteins?
Changes in pH, Increased Temperature, Exposure to UV light/radiation (dissociation of H bonds), Protonation amino acid residues, High salt concentrations are the main factors that cause a protein to denature.
Which of the following is a 39 residue hormone of the anterior pituitary gland?
ACTH
Adrenocorticotropic hormone (corticotropin; ACTH) is a 39-amino-acid peptide hormone produced by cells of the anterior pituitary gland and carried by the peripheral circulation to its effector organ, the adrenal cortex, where it stimulates the synthesis and secretion of glucocorticoids and, to a more modest extent.
Why would it be useful to determine the molecular weight of a protein?
Protein molecular weight is a key parameter to confirm, as the primary structure is the most foundational level of protein structure. Developing a robust understanding of the unmodified protein molecular weight can assist in initial assessments of the biomolecule’s functionality.
Why is the molecular weight of a protein important?
As the primary structure is the most foundational level of protein structure, protein molecular weight is a key parameter to confirm. Having a robust understanding of the unmodified protein molecular weight can help in initial assessments of the biomolecule’s functionality. This could include: Metabolic regulation.
Why do we use average molecular weight?
The molecular weight of a synthetic polymer does not have a single value, since different chains will have different lengths and different numbers of side branches. There will therefore be a distribution of molecular weights, so it is common to calculate the average molecular weight of the polymer.
Why is weight average molecular weight greater than number average?
More importantly, the weight average molecular weight is always greater than the weight average molecular weight since larger molecules in a sample weigh more than smaller molecules.
How is the molecular weight of a protein determined?
An apparent molecular weight (MW) of a protein can be determined from the migration distance of a protein complexed with a strong cationic detergent sodium dodecyl sulfate (SDS) separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
What is the average weight of an amino acid residue?
AAMC decided that we should know that an amino acid residue has an average weight of 110 Da which is equal to 110 g / mol for reference. IN is a 288-residue protein so it weights about 288 * 110 Da = 31680 Da.
What is the size of a tetramer with 288 amino acids?
The solution says that since the integrase monomer is composed of 288 amino acids, it will have a ~32 kDa, and thus the answer is 128 kDa for the size of a tetramer. How did they get the 32 kDa?? Is there a formula for this kind of question?
What is the molecular weight of an inactive tetramer of in?
There’s a question in the AAMC Section Bank that says that IN (integrase) is a 288-residue protein, and it’s asking what the molecular weight would be of an inactive tetramer of IN. The solution says that since the integrase monomer is composed of 288 amino acids, it will have a ~32 kDa, and thus the answer is 128 kDa for the size of a tetramer.
What makes glycine unique among the twenty amino acids?
3. Glycine is unique among the twenty amino acids because of its lack of chirality at the alpha carbon and its small side chain. This allows glycine to adopt conformations (phi, psi angles) which are inaccessible to the other amino acids.