1. To determine the sequence of amino acids in protein, partial hydrolyses at different points are made and then compared to other sets of partial hydrolyses For example: Complete hydrolysis gave: Phenylalanine-1 Histidine-2 Glutamic acid-1 Leucine - 4 Asparagine-1 Cystine -2 Glutamine-1 Glycine - 2 The Partial Hydrolyses yielded the following: 1st Hydrolysis : 4 polypeptides ● . IA: phe-val-asn-gln-his-leu IB: IC: leu-tyr-leu-val ID: val-cys-gly 2nd Hydrolysis: 3 polypeptides IIA: phe-val-asn-gIn-his-leu-cys-gly-ser-his-leu IIB: val-glu-ala-leu-tyr-leu IIC: val-cys-gly Write down the primary structure of this polypeptide by finding the overlaps of the amino acids therein: Serine-1 Valine-3 Alanine-1 tyrosine-1 cys-gly-ser-his-leu-val-glu-ala

What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.

The pka of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH 6.4? 15.3% 28.5% 45.3% O 66.6%

a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?

This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?

Using the picture provided, match the correct name of each of the functional groups highlighted in blue.

a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).

Your friend has discovered a protein that they suspect is glycosylated. They decide to perform a series of tests to determine the nature of the oligosaccharide. Assuming/Knowing the following: Fucose molecular weight is approximately 164 Galactose molecular weight is approximately 180 GalNAc molecular weight is approximately  221 Mannose molecular weight is approximately 180  Sialic Acid molecular weight is approximately 309 Neuraminidase cleaves before a Sialic Acid (Sialic Acid and anything after leaves the protein) Beta-galactosidase cleaves after a Galactose (Galactose and anything before remains on the protein) Peanut Agglutinin binds to GalNAc Concanavalin A binds to Mannose Hemagglutinin binds to Sialic Acid Based on preliminary results, they suspect that the oligosaccharide is 7 glycosides long and weighs a total of 1414 g/mol They carried out the following experiments: they treated the protein with either a glycosidase or a lectin, and then pelleted the protein using…

"Potassium Bromate (KBr03) is added to flour as a softener that strengthens the texture of bread. It can do this by forming disulfide bonds between two cysteine amino acids in a reaction similar to the chemical equation given below. The function of KBr03 is to remove the 2 electrons needed to form the disulfide bond as shown in the figure below. Each of the cysteine amino acids will be in a protein chain, so the reaction binds the two chains together, giving the dough cohesion. However, potassium bromate is a proven carcinogen and is only allowed in foods in the United States because bakers will add the right amount and correct It has been assumed to meet the temperature and cooking time conditions. " KBRO, + C,H¸NO,SH → KBr + H,O+C,H„N,O,S, Balance the reaction of potassium bromate (KBr03) with the cysteine molecule (C3H6 NO2 SH) by converting it into the reduced step matrix using the additive matrix method. (Kis the symbol of potassium in the question) (Homogeneous linear equation…

Create an oligopeptide via dehydration synthesis using the following amino acids. O. H Tryptophan (TRP) C-C-N но сн, C-C-N. но Glycine (GLY) H H HN