
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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PEPTIDE #1: Pro-Phe-Thr-Cys
PEPTIDE #2: Gly-Tyr-Ser-Asp
Calculate the pI of both peptides. Which is more acidic and why? Which one is more hydrophobic? Which peptide sequence (#1 or #2) would be more likely situated on the surface of the protein?
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- For each amino acid, show the structure, 1-letter abbreviation, 3-letter abbreviation, class (non-polar, polar, positive or negative), special props, side chain pKa)arrow_forwardWhat charge is carried by the peptide FREEENERGY at pH 7? (pKas: N-terminus: 9; C-terminus: 3; Arginine 11.6; Glutamic acid, 4.3)arrow_forwardConsider 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 = 12arrow_forward
- Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.arrow_forwardWhich of the peptide sequences below best matches the hydropathy plot shown? L 10 Residue Number 4 2 Hydropathy value -2 0 セー RAFLILFMTYFLILFLI ILYYAGSREDHSGYLIL OLHGDQNRERDGHSQERD EQSDTERNQHGALIYLI 01 5 15arrow_forwardI need help with drawing Hydrogen bonding between two tripeptide: Ser-Lys - Ser. In my class, we are required to give dash or wedge for the side chain R in the amino acid, and draw zig zag for the chain. In two separate drawings, can you draw one where it is the hydrogen bonding between the peptides backbone that connect the two tripeptides and the other is the hydrogen bonding between the side chains. Thanksarrow_forward
- A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recently isolated from the venom gland of a frog. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Acid Hydrolysis (6 N HC) at 10 C Heptapeptide (2) Arg. Pro, Phe, Tyr, Ala, Lys 2,4 dinitrafluerobenzene DNP-Phe Lys and modified free amino acids Peptide 1 (Ala, Lys) Cleovage with Trypsin, then chrometogrophy Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Peptide 4 (Arg. Tyr) Clevege with Chymetrypsin, then cromategrphy Peptide 5 (Lys, Pro, Ala, Arg)arrow_forwardPeptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE Which of these peptides would be most likely to be found as an a helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an a helix in a transmembrane protein? Which would be least likely to form an a helix of any kind? Briefly explain your answers.arrow_forwardif the tetrapeptide shown in the binding site above (Gly-Ser-His-lle) were in an aqueous solution at pH=6.2, what fraction of peptide molecules would have a +1 charge?arrow_forward
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