1 which parts of amino acids are involved in tertiary structures ? 2 polar side chain can make hydrogen bonds. Draw any polar side chain and a hydrogen bond to water. 3 what are the functional group of the basic amino acids? 4 what is the organic functional group in a peptide bond? 5 Do all protein have quaternary structure? 6 phenylalanine and valine are non polar amino acids. Do you think they are more likely to be found on the exterior or interior of a protein

1 which parts of amino acids are involved in tertiary structures ? 2 polar side chain can make hydrogen bonds. Draw any polar side chain and a hydrogen bond to water. 3 what are the functional group of the basic amino acids? 4 what is the organic functional group in a peptide bond? 5 Do all protein have quaternary structure? 6 phenylalanine and valine are non polar amino acids. Do you think they are more likely to be found on the exterior or interior of a protein

Biology: The Unity and Diversity of Life (MindTap Course List)

14th Edition

ISBN:9781305073951

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter3: Molecules Of Life

Section: Chapter Questions

Problem 6SQ

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1. what do you think a “peptide”means? 2. Proteins are extremely long, folded chains of amino acids, containing between 150-1000 amino acids linked together in a straight chain. A protein will have a long repeating chain of-N-C-C- as its backbone, with different R groups sticking out. How long could a protein be? be specific. 3. Add the C’s and H’s into their structural formulas. picture included
Please describe what is a peptide bond? What is the significance of the amino terminus versus the carboxy terminus? At which end are amino acids added to form a polypeptide, this is the term for linked amino acids? What are the 3 chemical groups that form an amino acid? A▾ B I I @ & 7
8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
3. Amino Acid Sequence and Protein Structure Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence. 1 3 5 6 7 8 9 10 Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala- - 11 12 13 14 15 17 20 Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp- 16 18 19 21 22 23 24 25 26 27 28 Gly - Met-Glu - Cys - Ala - Phe - His - Arg (a) Where might bends or ß turns occur? (b) Where might intrachain disulfide cross-linkages be formed? (c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, lle, Thr, Ala, Gln, Lys. Explain your reasoning.
Match the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondary
2. Two amino acids are shown below. Name them in the blanks, and then draw the structure of the dipeptide they would form if a peptide bond connected them (in the order shown.) Draw the dipeptide as a Zwitterion, and name it in the blank. H3N-CH- CH-C-O CH3 + + H3N-CH₂-C O
1. Hydrogen bonds can form an alpha helix or beta sheet. The hydrogen atom has a partial positive because of the atom it is covalently bound to. Name the two most common atoms hydrogen bonds within biological systems that give hydrogen a partial positive charge. 2. Are the atoms named in the question above in the backbone of the protein or are they found in R groups? Which R groups? 3. Besides hydrogen, what other atom is involved in the hydrogen bonds in an alpha helix or beta sheet? In other words, hydrogen is interacting with what other atoms when it makes a hydrogen bond? 4. Write out, in order, the full names of the seven amino acids circled in the picture.
1. Why do proteins become polycations at extremely low pH and become polyanions at very high pH? 2. Explain why hydrogen bonding is important to protein structure.
1. Draw NEW amino acids; name them and characterize them 2. Make two dipeptides with your two new amino acids. Name the two dipeptides. Indicate the peptide bond.
4. Each diagram in Figure 2 below shows one level of organization of a protein. Identify each level and describe it. CA ITA (a) (b) 0 hydrogen co CH₂ bond H-0 (c) -0, 0 lonic bond C-OH H₂C H₂C CH-CH₂ amino acids -hydrophobic interactions disulfide bridge Figure 2 5. Hemoglobin is made up of four polypeptides, but also require a beme group
3.Is the OH for the molecule in #2 from the carboxyl group or from the amino group?4.Is the H for the molecule in #2 from the carboxyl group or from the amino group?5.The splitting of a dipeptide into two separate amino acids would reverse the above reaction. What molecule would have to be added to a dipeptide in order to break a peptide bond and then split the dipeptide into two amino acids? (This kind of process in which water is added to a molecule when it splits apart is called hydrolysis.)
1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.