Homework Answers
Answer:
Unique-three-dimenstional shape of the full folded polypeptide
Explanation:
The tertiary structure of a protein results when a helix folded in specific fashions to give three dimensional or tertiary structure. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains.
Order in which amino acids are joined in a polypeptide chain ---Primary structure
Organization of a polypeptide chaint into an alpha-helix or beta-sheet---Secondary structure
Overall protein structure resulting from the aggregation of two or more polypeptide subunits---Quarternary structure
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Question 5 lp The tertiary structure of a protein is the unique three-dimensional shape of the...
Which sentence does describe definition of tertiary structure of proteins? A. Tertiary structure of proteins is...
Which sentence does describe definition of tertiary structure of proteins? A. Tertiary structure of proteins is defined as amino acid sequence of their polypeptide chain(s) B. Tertiary structure of proteins is defined as regular set up of their polypeptide chain(s) to form a-helix or b-sheets. C. Tertiary structure of proteins is defined as spatial set up of domains of proteins linked by peptide bounds. D. Tertiary structure of proteins is defined as spatial set up of subunits of...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to higher order Primary structure describes the order of amino acids in the peptide chain. Secondary structure describes the basic three-dimensional structures, a-helices and B sheets. Tertiary structure describes how the secondary structures come together to form an individual globular protein. Quatemary structure results from individual proteins coming together to form multi-subunit protein complexes Part A Complete the following vocabulary exercise relating to the level...
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative...
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative polarity of their side chain. Consider a folded protein in an aqueous environment; where would the hydrophobic amino acids likely be found? -Tucked away in the middle of the folded protein -Randomly distributed throughout the protein -Exposed on the exterior surface of the folded protein 2. All proteins exhibit a primary, secondary, and tertiary structure, but not all proteins exhibit a quaternary structure. Describe...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks that are referred to as regular secondary structures, Some proteins have alpha-helices, some have beta-sheets, and still others have a combination of both. What makes it possible for proteins to have these common structural elements? 12 15 a) the hydrophobic-core interactions. b) hydrogen bonds that form along (alpha helices) or between (beta sheets) polypeptide backbones. c) side-chain interactions d) specific amino acid sequences. 7...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereoce...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereocentre). (b) What is the significance of chirality in the biological world? 7. (a) Sh (a) Show the repeating unit of the polypeptide chain in a protein and indicate the peptide bond. (b) What are the following structures of a protein (i) primary, (ii) secondary, (iii) tertiary and (iv) quaternary. 1. Polypeptides are the natural polymer of the naturally...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys,...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
The _______ of amino acids in a protein is referred to as its primary structure
24. The _______ of amino acids in a protein is referred to as its primary structure. A) twisting B) sequencing C) folding D) none of these 25. The structure of a protein is most important because the _______ of the amino acids determines its overall shape, function and properties. A) primary, twisting B) primary, sequencing C) secondary, twisting D) secondary, folding E) none of these 26. The secondary structure of a protein is due to_______ between amino acid residues. A) hydrophobic interactions B) hydrogen bonding...
QUESTIONS The primary structure of a protein is the result of which of the following bond...
QUESTIONS The primary structure of a protein is the result of which of the following bond types? O A amide bond B. hydrophobic interactions o disulfide bond D. hydrogen bond QUESTION 6 Quaternary structure is associated with A the sum of the secondary and tertiary structures B. the relative orientation of one polypeptide to another polypeptide in a multisubunit protein o the formation of the primary structure D. the shape of the polypeptide chain
added part a of the question for clarity 1. Polypeptides are the natural polymer of the...
added part a of the question for clarity
1. Polypeptides are the natural polymer of the naturally occurring amino acids. Their structure can be considered at various levels to consist of Primary: amino acid sequence secondary: regions of ordered structure (a-helix, B-sheet, etc.) tertiary: overall 3D shape; folding quarterniary: interaction of protein sub-units (a) Consider the following segment of a polyamide H Show the resonance structures for the amide bond (in the box) (i) (ii) Indicate what o and w...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to higher order Primary structure describes the order of amino acids in the peptide chain. Secondary structure describes the basic three-dimensional structures, a-helices and B sheets. Tertiary structure describes how the secondary structures come together to form an individual globular protein. Quatemary structure results from individual proteins coming together to form multi-subunit protein complexes Part A Complete the following vocabulary exercise relating to the level...
Question 10 (4 points) Although all protein structures are unique, there are common structural building blocks that are referred to as regular secondary structures, Some proteins have alpha-helices, some have beta-sheets, and still others have a combination of both. What makes it possible for proteins to have these common structural elements? 12 15 a) the hydrophobic-core interactions. b) hydrogen bonds that form along (alpha helices) or between (beta sheets) polypeptide backbones. c) side-chain interactions d) specific amino acid sequences. 7...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereocentre). (b) What is the significance of chirality in the biological world? 7. (a) Sh (a) Show the repeating unit of the polypeptide chain in a protein and indicate the peptide bond. (b) What are the following structures of a protein (i) primary, (ii) secondary, (iii) tertiary and (iv) quaternary. 1. Polypeptides are the natural polymer of the naturally...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
QUESTIONS The primary structure of a protein is the result of which of the following bond types? O A amide bond B. hydrophobic interactions o disulfide bond D. hydrogen bond QUESTION 6 Quaternary structure is associated with A the sum of the secondary and tertiary structures B. the relative orientation of one polypeptide to another polypeptide in a multisubunit protein o the formation of the primary structure D. the shape of the polypeptide chain
added part a of the question for clarity
1. Polypeptides are the natural polymer of the naturally occurring amino acids. Their structure can be considered at various levels to consist of Primary: amino acid sequence secondary: regions of ordered structure (a-helix, B-sheet, etc.) tertiary: overall 3D shape; folding quarterniary: interaction of protein sub-units (a) Consider the following segment of a polyamide H Show the resonance structures for the amide bond (in the box) (i) (ii) Indicate what o and w...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
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