Name the two different glycosidic linkages.  Are these the same linkages as those found in glycogen?

is it true that aplha and beta are made up of same amino acids but Beta chain is longer than alpha chain？what is other difference and similarity？is the amino aicd sequence exactly the same as well？are their structure the same ？

With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).

(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes.   Answer (iii) to (v) please.

Draw the structural formula of the oligopeptide if the amino acids are arginine, glutamine, glycine, methionine and glutamic acid considering the first amino acid is the N-terminus

Draw the tetrapeptide Met-Ile-Lys-Glu at a ph of 7?

Polylysine adopts a random structure in solution at physiological pH (i.e. 7.4). Given that the e-amino group of lysine has a pKa of 10.5, under what circumstances do you think polylysine will form an a-helix? Give an explanation for your decision.   Given the pKa of the side-chain COOH group, under what circumstances would you anticipate polyglutamate to form an a-helix?

Hemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer Using the size-exclusion chromatogram given, 1.  Draw an SDS-Page Gel with a reducing agent such as BME using the three peaks listed on the graph.

What would the following sequence of dodecapeptide M be? My best guess would be option C

Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below,  please show them in zig-zag style, from amino to carboxy terminus, with correct  stereochemistry Draw the predominant form at pH = 2  Draw the predominant form at pH = 5  Draw the predominant form at pH = 7  Draw the predominant form at pH = 12