=> Due to the interactions of Cations and Anions with the salt
Proteins may be thought of as beads (amino-acids), forming a chain. Proteins fold into their final shape because some of these beads are hydrophobic amino-acids which want to get out of water and pack up against other hydrophobic amino acids (grease likes grease and not water). This process is called hydrophobic collapse. The amino acids also have an electrostatic component and need to pack up against other electrostatic components. In high salt concentration, one disrupts the electrostatic interactions because the salt competes for the electrostatic interactions within the protein weakening them. Some salts also disrupt the structure of water which weakens the interactions pushing the protein into its shape. In summary, depending on the salt and the concentration, salt can denature a protein by competing for electrostatic interactions within the protein replacing them with protein-salt interactions or disrupt the structure of water that allows both the grease and charge to weaken.
Question 30 How can a highly concentrated salt denature a protein? Due to the increase in...
How can a highly concentrated salt denature a protein? Due to the increase in the pH. Due to the mechanical forces involved Salts can't never denature a protein Due to the interactions of cations and anions with the salt estion 31 mahelix and beta pleated sheets are examples of which level of protein structure zero order
QUESTION 7 Which of the following does not cause a protein to denature? O A heat 0 B. pH o detergent D. None of the above QUESTION 8 Repeating structural motifs, which make up secondary structures, such a alpha helices and beta sheets, are predominantly formed as a result of A hydrophobic interactions B. peptide bonds oC electrostatic interactions D. intramolecular hydrogen bonding QUESTION 9 Hydrophobic interactions could occur be Avaine and a nine B. aspartate and argnine C glutamine...
9. Alpha-helices and B-pleated sheets are both examples of a. primary structure. b. secondary structure. c. tertiary structure. d. quaternary structure. 14. The most common moti uispersion forces nost common motifs for this level of structure are the helix and the B- pleated sheet a. primary structure b. secondary structure c. tertiary structure d. quaternary structure e. both secondary and tertiary of a protein. 15. The amino acid sequence is the a. primary structure b. secondary structure c. tertiary structure...
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino acid sequence defines the native structure of protein. b.) What is the main type of bonding responsible for stabilizing the secondary structure of proteins? c.) Briefly discuss the thermodynamics of protein folding into its native 3D structure. Is this process enthalpy driven or entropy driven? d.) Give an example of 2 major secondary structural motifs found in polypeptides. Do any of these motifs appear...
Question 1
The protein in the diagram is (circle all that apply):
Group of answer choices
a) a peripheral membrane protein
b) an integral membrane protein
c) a lipid anchored protein
Question 2
The protein shown in the diagram could potentially function as
(circle all that apply):
Group of answer choices
a) a receptor
b) a transmembrane anchor
c) a pore or channel
Question 3
The protein shown in the diagram has which of the following
(choose all that apply)?...
10. Write a one-page summary of the attached paper? INTRODUCTION Many problems can develop in activated sludge operation that adversely affect effluent quality with origins in the engineering, hydraulic and microbiological components of the process. The real "heart" of the activated sludge system is the development and maintenance of a mixed microbial culture (activated sludge) that treats wastewater and which can be managed. One definition of a wastewater treatment plant operator is a "bug farmer", one who controls the aeration...