1. Describe the types of interactions that keep complex structures of proteins intact and explain AT...
1. Describe the types of interactions that keep complex structures of proteins intact and explain AT LEAST two of the general rules governing tertiary folding in terms of amino acid distribution and polypeptide chain trends/structure.
Homework Answers
The interactions that keep complex structures of protein intact are Non covalent interactions like Hydrogen bonding i.e (dipole-dipole interaction between H and electronegative atom attached in Amino acids like N (H--N)), ionic interactions, and hydrophobic interactions. Moreover, they have some sorts of covalent bonding includes disulphide interactions especially in cystein.
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1. Describe the types of interactions that keep complex
structures of proteins intact and explain AT...
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...
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...
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)...
Which of the following statements Explain primary, secondary, tirtially and quaternary structures of protien Questions for...
Which of the following statements Explain primary,
secondary, tirtially and quaternary structures of protien
Questions for G2: 1) Would you expect to find valine and leucine on the outside or the inside of the tertiary structure? Why? pts) 2) State whether the following statement describe primary, secondary, tertiary, or quaternary protein (15 pts) structure A. Adjacent chains of polypeptides are held together by hydrogen bonds between the O of the carbonyl group of one chain and the H of an...
pls answer 6 and 7 6. Secondary structure (turn): The image below is of a polypeptide...
pls
answer 6 and 7
6. Secondary structure (turn): The image below is of a polypeptide in secondary (20) structure level of protein folding. Specifically it is of a turn. Turns vary in length. The shorter the turn the more drastic the angle changes. The longer the turn, the more gradual the angles needed. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? Is this bond/interaction permanent or transient? d. What parts...
Describe the four categories of amino acid side chains. What types of interactions are the members...
Describe the four categories of amino acid side chains. What types of interactions are the members of each of these categories likely to make? Now describe and explain the four levels of protein structure, giving a specific example of each an how amino acids are involved.
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...
Please explain Why is a cap added to MRNA, but not to 1RNA or RRNA? Each...
Please explain
Why is a cap added to MRNA, but not to 1RNA or RRNA? Each of the three types of RNA are transcribed by different RNA polymerases. Only RNA polymerase II, involved in mRNA synthesis, contains a domain capable of interacting with enzymes that form the cap. Transcription and processing of MRNA occur in the nucleus, where cap binding proteins are found. These proteins, which add and modify the cap, are not found in the cytoplasm, where tRNA and...
please answer! 3) Protein structure and amino acid side chains a) Give examples of the types...
please answer!
3) Protein structure and amino acid side chains a) Give examples of the types if attractive forces found between the side chains of the following amino acid residue pairs at pH 7.4 00 Leu and Phe (ii) Two Cys (ii) Asp and Thr (iv) Asp and Arg b) Of the 4 levels of protein structure, which ones are stabilized by interactions between amino acid side chains? c) Identify the two regular types of secondary structures and describe the...
Proteins are polymers of amino acids that can exist in ordered structures stabilized by a variety...
Proteins are polymers of amino acids that can exist in ordered structures stabilized by a variety of molecular interactions. However, when certain conditions are changed, the compact structure of a polypeptide chain may collapse into a random coil. This structural change may be regarded as a phase transition occurring at a characteristic transition temperature, the melting temperature, Tm, which increases with the strength and number of intermolecular interactions in the chain. A thermodynamic treatment allows predictions to be made of...
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)...
Which of the following statements Explain primary,
secondary, tirtially and quaternary structures of protien
Questions for G2: 1) Would you expect to find valine and leucine on the outside or the inside of the tertiary structure? Why? pts) 2) State whether the following statement describe primary, secondary, tertiary, or quaternary protein (15 pts) structure A. Adjacent chains of polypeptides are held together by hydrogen bonds between the O of the carbonyl group of one chain and the H of an...
pls
answer 6 and 7
6. Secondary structure (turn): The image below is of a polypeptide in secondary (20) structure level of protein folding. Specifically it is of a turn. Turns vary in length. The shorter the turn the more drastic the angle changes. The longer the turn, the more gradual the angles needed. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? Is this bond/interaction permanent or transient? d. What parts...
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...
Please explain
Why is a cap added to MRNA, but not to 1RNA or RRNA? Each of the three types of RNA are transcribed by different RNA polymerases. Only RNA polymerase II, involved in mRNA synthesis, contains a domain capable of interacting with enzymes that form the cap. Transcription and processing of MRNA occur in the nucleus, where cap binding proteins are found. These proteins, which add and modify the cap, are not found in the cytoplasm, where tRNA and...
please answer!
3) Protein structure and amino acid side chains a) Give examples of the types if attractive forces found between the side chains of the following amino acid residue pairs at pH 7.4 00 Leu and Phe (ii) Two Cys (ii) Asp and Thr (iv) Asp and Arg b) Of the 4 levels of protein structure, which ones are stabilized by interactions between amino acid side chains? c) Identify the two regular types of secondary structures and describe the...
Proteins are polymers of amino acids that can exist in ordered structures stabilized by a variety of molecular interactions. However, when certain conditions are changed, the compact structure of a polypeptide chain may collapse into a random coil. This structural change may be regarded as a phase transition occurring at a characteristic transition temperature, the melting temperature, Tm, which increases with the strength and number of intermolecular interactions in the chain. A thermodynamic treatment allows predictions to be made of...
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