Question

14. What is Hydrophobicity Scale? Classify the amino acids according to this scale. How do surface and core a protein differ? 15. Describe the three common ways to stabilize protein structures? 16. What are some substances that will denature proteins? How do they cause denaturation? How can renaturation of a protein be brought about? 17. What is the function of molecular chaperones?

Answer 1

14. Hydrophobicity scale are values that define relative hydrophobicity of amino acid residues. The more positive the value of this Scale → the more hydrophobic are the amino acids located in that region of the protien. Core protein & The amino acids in the interior more are on average hydrophobic than the residual on the surface. - Protein core is the part of a folded protech with Zero-solvent accessibility Surface Proteins : surface proteins are proteins that are embedded in or span the layer of cell membranes of more complex organisms. 3) Those protiens are integral to the way in which a cell interacts with the environment around it, including other cell. = Some of those protions, especially omes that are exposed to the external side of the membrane, are called glycoproteins because they have carbohydrates attached s tenta di without er surfaces. CamScanner

15 Structure & stability of protein are strongly dependent on the arrangements & the hydrophobic core - the sequence of habophobic Amino acid residues in the backbone of the protien. =) Tertiary structure is formed by interaction between side chain of various amino acids - in particular disulfide bonds formed between two cysteine groups. - The C-N bond in an amino acid's chain has the character of a double bond. This bond has a short length and stable, Scanned with CamScanner

e naturation Ans 16 is a process in which protiens ex lose the quaternars tertiary & secondary Structure is present in their native State. Ex. Strong Acid or Base (mean pH is o affect the protien structure. ) - Concentrated in organic salts. an organic salt (e.g. alcohol or chloroform) Temprature (radiation or heat) = Renaturation in molecular biology refers to the reconstruction of a protein. or nucleic acid ( such as DNA) to their original form especially after denaturation This process is therfore the inverse of denaturation. In denaturation, the proteins lose their native biomolecular structure, or Reconstructing the denatured Acid or protein into its original form is done as smyned then process or renaturatico, CañScanner

17 Molecular chaperones are protions that assist the covalent folding or unfolding a the assembly or disassembly of other makromolecular structures. function & major function of chaperones is prevent both newly synthesised polypeptide chain and assembled suf writs from aggregating into nonfunctional structures, Mote Macromolecular Crowding may be important in chaperone fraction. The crowded environ- ment of the cytosol can accelerate the folding) process, since a compact forded protein will occupy less volume than unfolded proteen chain. However, crowding can reduce the yield of correctly folded : protein by increasing protein aggregation. crowding at may also increase the effective ness of the chaperone postaens och Scanned with CamScanner