On a sheet of paper , sketch a picture of a dehydration synthesis reaction between two amino acids. This is not meant to be tricky! Use Fig. 3.18 as a model. Be sure to identify what specific atoms on each amino acid will be involved in the reaction, and be sure and show the solid line that denotes the new covalent bond that will exist in the product. On one of your amino acids, label the amino group, the carboxyl group, and the side chain. FInally, point to and label the peptide bond in the resulting dipeptide. Take a picture of your lovely drawing and upload it here. LARGE BIOLOGICALMOLECULESV Figure 3.18 The structure of a protein. The chain below,drawn in serpentine fashien so that it fits on the page, shows theamino acid sequence of a polypeptide found in lysozyme, anenzyme in your tears and sweat that helps preventbacterial infections. The names of the amino acidsare given as their three-letter abbreviations; forexample, the amino acid alanine is abbreviated"ala" This amino acid sequence folds into aprotein of specific shape, shown at bottomin two computer-generated representa-tions. Without this specific shape, theprotein could not perform its function.H.HN=C=CHO.CH2OHOne amino acid (alanine)LE Ala AlaAlaLysAng)fhe AsLys AlaAsnAgAsn (TheAsnCys-Le-Asn-Arg-SerThr-Arget-alinofromlethe AlaCysAsn)129The amino acid sequence of lysozymeLethestruc-

There are twenty standard amino acids that are used to make all the proteins synthesized inside the…

On a sheet of paper , sketch a picture of a dehydration synthesis reaction between two amino acids. This is not meant to be tricky! Use Fig. 3.18 as a model. Be sure to identify what specific atoms on each amino acid will be involved in the reaction, and be sure and show the solid line that denotes the new covalent bond that will exist in the product. On one of your amino acids, label the amino group, the carboxyl group, and the side chain. FInally, point to and label the peptide bond in the resulting dipeptide. Take a picture of your lovely drawing and upload it here.

On a sheet of paper , sketch a picture of a dehydration synthesis reaction between two amino acids. This is not meant to be tricky! Use Fig. 3.18 as a model. Be sure to identify what specific atoms on each amino acid will be involved in the reaction, and be sure and show the solid line that denotes the new covalent bond that will exist in the product. On one of your amino acids, label the amino group, the carboxyl group, and the side chain. FInally, point to and label the peptide bond in the resulting dipeptide. Take a picture of your lovely drawing and upload it here.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter30: Protein Synthesis

Section: Chapter Questions

Problem 18P

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Similar questions

Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
a 3d structure of protein with acces number of P02008 at uniprot database.
01 Description Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): NH₂ OH Alanine H H O OH Proline lysine alarmy stock płwłos Tryptophan OH COOH | H₂N-C-H CH₂ Phenylalanine arginine
E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o
Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can form only under certain conditions (oxidative conditions). We'll talk about oxidation and reduction next week. For now, just note that this type of bond does exist in some proteins. Answer the below questions on tertiary structure in your own document. 8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a protein (labeled A, B, and C). Do these interactions involve only the amino acid R groups, only the polypeptide backbone atoms, or both? 9. In the table below, indicate what type of bond/ interaction is represented in the examples shown in Figure 6, panels A, B, and C and whether each interaction involves group or backbone atoms. Example Type of Bonding Interaction R group or backbone? A В 10.…
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm
Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminus
BIOLOGICAL MACROMOLECULES Identifying the major types of RNA from a description Check the box under each molecule for which the statement in the first column is true. statement In order to do its job, it must have an amino acid attached. When attached to a ribosome, it "reads" each codon in a messenger RNA and supplies the matching amino acid. It has a sugar-phosphate backbone to which are attached many adenine, uracil, cytosine, or guanine bases. When attached to a DNA molecule, it causes the process of replication to begin. It's made in the nucleus, and unlike other nucleic acids remains there to do its job. 0/5 messenger ribosomal RNA RNA 0 Israel 0 ▸ Odlo Ar BA
GTTTTCACTGGCGAGCGTCATCTTCCTACT 10. Generate a secondary structure prediction for one identified protein.
STRUCTURE OF DNA Phosphate Nitrogenous Base Pentose Sugar Referring to the illustration above, the entire molecule shown is called a(n): O polysaccharide O amino acid O pyrimidine O nucleotide
TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
Accoding to the figure below, which amino acid will be added next to the growing polypeptide chain? 5' AÚG UUC GGU AAG 3' ÁÁĞÚĞÁ UAC Peptide bond formation Tryptophan (Trp) Glycine (Gly) Methionine (Met) Leucine (Leu) Phenylalanine (Phe) O O