Consider the structure of the amino acid L-asparagine.Part 1 of 3Draw the structure of L-asparagine at pH-6.Part 2 of 3Click and drag to start drawing astructure.Draw the structure of L-asparagine at pH-2.Part 3 of 3Click and drag to start drawing astructure.Draw the structure of L-asparagine at pH-10.Click and drag to start drawing astructure.奶+GD:x5xA :0Q

L- asparagine at pH=6there were technical glitches from this site to upload the online generated…

Answered: Consider the structure of the amino…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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draw a “trans” and a “cis” peptide bond of alanine and threonine with the peptide bond lying in the plane of the paper. Draw a second view of each peptide bonds now looking down/along the peptide bond (i.e. one atom of the peptide bond will be in front and will obscure the second one behind it). Using a circular arrow, demonstrate how the torsion angle can be directly “read” from the picture. You can do this with an accuracy of ~10°. Provide an explanatory caption.
what is the n-terminal AA residue? use one-letter code for amino acid
what is the c-terminal AA residue? use one-letter code for amino acid
What to submit: Draw in the hydrogen bonds for parallel and antiparallel sheets and replace the current image with new ones. Underline the correct sheet type. Submit as an image or PDF. Label the amino acids in the following peptide using their three-letter and one letter code H₂N OH Three Letter Code - One Letter Code - ZI IZ ZI NH₂ Draw out the following peptide (CHARLIE) from N to C terminus. Draw by hand and upload as a file attachment. What is the net charge of your peptide? net charge:+
Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation. Polyglutamate, a polypeptide made up of only l-Glu residues, is an α helix at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (l-Lys residues) is an α helix at pH 10, but when researchers lower the pH to 7, the specific rotation also decreases, as shown in the graph. The graph plots pH on the horizontal axis ranging from 0 to 14, labeled in increments of 2, against specific rotation on the vertical axis. The curve for poly (Lys) begins as a horizontal line just above the horizontal axis. This is labeled, random conformation. At 8.5, it bends sharply upward and becomes diagonal at 8.8 until 9.9, when it reaches a height of two-thirds of the height of the…
Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids. ___1___--_2_- 3 -- --__6_--_7__ a. The amino acid in the C-terminal is optically inactive. b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein but produces a yellow soln with basic hydrolysate. It also gives a negative result with both Hopkin's Cole and Millon's test using basic hydrolysate. c. After treatment of this peptide with aminopeptidase (specificity: peptide bond on the N-terminus), it yields serine and a hexapeptide d. The amino acid besides the N-terminal amino acid. will yield ornithine and urea after alkaline hydrolysis. e. The third amino acid gives a positive result for Hopkins-Cole Test. f. Chymotrypsin^ cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue. g. The amino acid at the carboxy-end of the third amino acid will yield a…
I'm conducting an experiment concerned with the binding affinity of tretinoin (all trans retinoic acid) and beta lactoglobulin. This can be accomplished by monitorization of fluorescence quenching of a tryptophanyl residue that resides in a hydrophobic pocket known as a calyx inside the protein. Generally, fluorescence quenching is classified as static or dynamic. Would fluorescence quenching be a result of amide bond formation to tryptophan from tretinoin or through another mechanism (ie FRET: Forester resonance energy transfer)? Could it be both?
The amino acid sequence (primary structure) and 3D shape (tertiary structure) of the rhodopsin has been determined and the various protein domains have also been identified with precision (see figures below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 cytoplasmic side extracellular side CH3 Retinal CH3 Rhodopsin (primary structure) C-II H 500000 NOOⓇ ...ooo E-II COOH-terminal C-III ago E-III CONJOO NH₂-terminal Rhodopsin + retinal (tertiary structure) 5. Based on the molecular structures of retinal, which of the following is the most likely? A. Retinal is an enzyme B. Retinal is a phospholipid of the plasma membrane C. Retinal is an unsaturated organic compound D. Retinal is a transport protein that moves a molecule across…
The amino acid sequence (primary structure) and 3D shape (tertiary structure) of the rhodopsin has been determined and the various protein domains have also been identified with precision (see figures below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 CH3 cytoplasmic side Retinal C-I extracellular side 0000 MOO OOO 400 DERY 000 PONE ALMO VOO LGF LLOD VUEL CH3 HOO AD SLV GO04 FAV OCK 000 LOO GOF YO DOAA TOTO ⓇAD MOWE OV00 OPL ALA LEGE DOOD VOOO COP DES 000 600 GCO OV FOOD Rhodopsin (primary structure) C-II E-II COOH-terminal C-III RIVE OOM DOWO LWCO 40 DOVO FOX ON DO 000 D04 boooooo 000 000 100,00 ****** E-III NH₂-terminal Rhodopsin + retinal (tertiary structure) 6. This lysine (K) is in a transmembrane domain of rhodopsin…
For each polypeptide derived in the following sequences: 5' CAA GAG GUA UCC UAC AGA 3' 5' GUC AUC UGG AGG GGC AUU 3' 5' CUA UGC AGU AGG ACA CCC 3' 1. Draw the structure of each polypeptide. 2. Label the amide bonds. 3. Identify the N-terminal and C-terminal amino acids. 4. Write the name of each polypeptide.
A tridecapeptide yields the following fragments when partially hydrolized. Determine the sequence of amino acids in the tridecapeptidedrolyzed. Determine the sequence of the tri decapeptide. tridecapeptide à lys-arg + gly-phe-pro + phe-ser-asp-lys + pro-phe-ser + asp-lys-arg-val + gln-ala-tyr + val-trp-gln. Determine the sequence of amino acids in the tridecapeptide
You were able to extract an amino acid sequence from an unknown protein you process through mass spectrophotometry. How will you able to identify the said protein and its function?

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