Discuss how considering 'allylic strain' can explain the favoured conformation of alanine in the tripeptide Ala-Met-Thr, and how this is relevant to the B-sheet conformation in peptides/proteins.
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Discuss how considering 'allylic strain' can explain the favoured conformation of alanine in the tripeptide Ala-Met-Thr, and how this is relevant to the B-sheet conformation in peptides/proteins.
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- draw the structure of the peptide Asp - Asn-Ser-Lys-Pro at PH 8Determine the isoelectric point of the peptide product of the mutated sequence: 5' - AUG UCC AUG AUU CUG GAA AUU ACC UCC AUC AUG AAG CGC UGA CCC AUU AUU AA - 3'How do you think incorporating b-homoserine into a peptide would affect the structure and/or polarity of the peptide compared to a serine residue?
- Illustrate the titration curve of the peptide with the given sequence below. Show the pKas, equivalence points, and approximate pI. Threonine-Leucine-Serine-Alanine-Arginine-Isoleucine-Aspartic Acid-ValineA heptapeptide when treated with trypsin produced two peptides. T1 (D, G, Y) and T2 (K, F, V, A). When the heptapeptide was treated with chymotrypsin, three peptides were produced: CT1 (K,,Y, G), CT2 (F,A, V), and CT3 (D). The sequences of these peptides is not known, however. When the peptide was treated with Sanger’s Reagent and hydrolyzed, DNP-K and DNP-A were recovered. What is the amino acid sequence of the heptapeptide?A sample of a peptide of unknown sequencewas treated with trypsin; another sample of the same peptide wastreated with chymotrypsin. The sequences (N-terminal to C-terminal)of the smaller peptides produced by trypsin digestion were as follows:
- Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5 equivalnets of KOH (Please type answer)Hypoxanthine can also base-pair with cytosine. Draw the structure of this base pair.How do you think incorporating a-methylserine into a peptide would affect the structure and/or polarity of the peptide compared to a serine residue?
- In pyrimidine nucleosides, the anti conformation predominates. Explain. Do the purine nucleosides have similar interactions?What might be an explanation for how the human protein binding to pili protects against a UTI?In addition to in the information given in the pictures, researchers provide further descriptions for the figure stating: Players were also able to restructure b-sheets to improve hydrophobic burial and hydrogen bond quality. Automated methods have difficulty performing major protein restructuring operations to change b-sheet hydrogen-bond patterns, especially once the solution has settled in a local low-energy basin. Players were able to carry out these restructuring operations in such scenarios as strand swapping (Fig. 3) and register shifting. In one strand-swap puzzle, Foldit players were able to get within 1.1 A° of the native structure, with the top-scoring Foldit prediction being 1.4 A° away. A superposition between the starting Foldit puzzle, the top-scoring Foldit solution, and model 1 of the native NMR structure 2kpo (Protein Data Bank) are shown in Fig. 3b. Rosetta's rebuild and refine protocol, however, was unable to get within 2 A ° of the native structure (Fig. 3a, yellow…