Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Phe: F Gly, Ser, Thr, Cys, Tyr, Asn Gln Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle:I Trp: W Туг: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense

Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Phe: F Gly, Ser, Thr, Cys, Tyr, Asn Gln Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle:I Trp: W Туг: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense

Body Structures & Functions

12th Edition

ISBN:9781285695495

Author:Scott

Publisher:Scott

Chapter3: Cells

Section: Chapter Questions

Problem 5C

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Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
For each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167
A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?
A peptide containing 18 amino acid residues in its sequence was partially hydrolyzed and peptides A–D were detected in the resulting mixture. Draw the sequence of the original peptide.A Phe-Gly-AlaB Ser-Ser-Ser-Trp-Phe-Gly-AlaC Phe-Phe-Met-Ala-Ala-Pro-Trp-CysD Met-Ala-Ala-Pro-Trp-Cys-Leu-Ile-Leu-Ser-Ser
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
Of the following amino acids, which 3 are most likely to be found on surface of a single protein. a) Arg b) Trp c) Cys d) Phe e) Leu f) Lys
A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
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 Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
Draw the bond-line structure of the given peptides. 1. Ser-Asp 2. Glu-Gln 3. Arg-His 4. Ala-Val-Ser 5. Glu-Gln-Gly 6. Cys-Gly-Asn
What is the overall charge on peptide AVGDWESKELLE at pH 7.0? a. -3 b. -2 c. 0 d. +1 Which of these decapeptide is the most hydrophobic? 1. ADEEEHNRQL 2. AVLKTIFYRS 3. AVLTIIFYRG 4. AVLTDNQLPK
The amino acid sequence of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH =7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listen in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an alpha helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an alpha helix in a transmembrane protein? Which would be least likely to form an alpha helix of any kind?