Describe what type of information the following views provide about protein structure determination?
a. Secondary structure:
b. Cartoon :
c. Composition
d. Hydrophobic/Polar
e. Charge
Secondary structure of protein:- The secondary structure of protein includes arrangement of peptie bonding or stretching of peptide bond for protein molecule. It can be done in two ways alpha helix & beta pleated sheet.
Alpha helix structure:- It is a right handed coiled strand. The side chain of amino acid groups are towards the outside of alpha helix. Hydrogen bonds form between the oxygen of the carbonyl group (>C=O) and the hydrogen atom of the N-H group of the peptide bond four amino acids below it in the helix. Hydrogen bonds give stability to the structure.
Beta pleated sheet structure:- In this either parallel or antiparallel depending on the directions of N-terminus to C-terminus on the same or opposite directions. The carbonyl oxygen of >C=O group hydrogen bonded with hydrogen atom of amino terminus.
Cartoon:- It is useful in analysing and understanding complex protein folds.
Composition:- Proteins are made up of amino acids. Amino acids composition vary as it grouped as sulphur containging, basic amino acids, acidic amino acids, aromatic amino acids, imino group, branched chain. These gives protein differentiation for their structure, function.
Hydrophobic/polar:- Due to Hydrophobic nature proteins can be folded it gives compact shape to protein.
Chargge:- Depending on the charge of amino acid the interactions are takes place for folding the protein to give proper confirmation. It includes covalent interactions, Vander waals forces, hydrophobic interaction, disulfide bond these are involved and takes place in secondary and tertiary structure of protein.
Describe what type of information the following views provide about protein structure determination? a. Secondary 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...
List and describe the two approaches to determining the tertiary structure of a protein. Experimental Determination Computational prediction There are three methods of computational structure prediction. Define each of the methods and describe when each method would be used. There are three types of helices formed by the secondary structure of protein. List three helices and rate how tightly coiled they are. Explain your reasoning. Choose any three of the twenty amino acids. Based on what you know about the...
25) What maintains the secondary structure of a protein? a) hydrophobic interactions b) hydrogen bonds between the R groups c) peptide bonds d) disulfide bonds e) hydrogen bonds between the amino group of one peptide bond and the carboxyl group of another peptide bond
The type of bond that is most important in maintaining secondary structure of a protein is disulfide bridges hydrogen bonding between R groups hydrogen bonding within the backbone salt bridges hydrophobic interactions metal ion coordination QUESTION 2 A glycerophospholipid with the phosphate ester group bonded to ethanolamine would be classified as a cephalin lecithin sphingomyelin cerebroside ganglioside
What kinds of interactions are NOT part of tertiary protein structure? 3 . A) salt bridges In a hydrolysis reaction, B) hydrophilic interactions A. an acid reacts with an alcohol. C) disulfide bonds E. an este reacts with NaOH. C. anester reacts with H.O. D) peptide bonds D. an acid neutralizes a base. E) hydrophobic interactions E. water is added to markene. . All amino acids have chiral Carbon atoms except a. Val 6. Lys C. ASP d. Ala e....
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.
The type of bonding that maintains the secondary structure in a protein is theA) Hydrogen bonds between the carbonyl and amino groups of the backboneB) Covalent bond between the carbonyl and amino groups of the amino acidsC) Hydrogen bonds between two amino acidsD) Disulfide bonds that hold two polypeptide chains togetherE) Hydrogen bonds between two amino groups
A protein with quaternary structure a. has twice the normal amount of secondary structure b. contains only four types of amino acids c. is not stabilized by the hydrophobic effect d. contains more than one subunit
The protein structure labeled A is , whereas, the structure labeled B is Proteins O a) All of the above Ob) Amphipathic, polar C) Hydrophilic, hydrophobic d) Hydrophobic, hydrophilic
Predict what would happen to the secondary structure of a protein if an alcohol that disrupts hydrogen bonding were added. Choose one or more answer (if applied): A. Nothing would happen to the protein; hydrogen bonding is not important for secondary structure B. The beta sheets would unfold, disrupting protein structure C. The a helixes would unfold, disrupting protein structure D. Individual amino acids would be hydrolyzed from the protein, disrupting protein structure