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2. The amino acid side chain residues in an a helix point center of the helix. A) Outward B) Inward C) Perpendicular D) Horizontally away from the

2. The amino acid side chain residues in an a helix point center of the helix. A) Outward B) Inward C) Perpendicular D) Horizontally away from the

Anatomy & Physiology
Anatomy & Physiology
1st Edition
ISBN:9781938168130
Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Publisher:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Chapter2: The Chemical Level Of Organization
Section: Chapter Questions
Problem 36CTQ: Explain why CH4 is one of the most common molecules found in nature. Are the bonds between the atoms...
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Name : Surname: 2. 3. 4. The amino acid side chain residues in an a helix point center of the helix. A) Outward B) Inward C) Perpendicular D) Horizontally Please I need the solution in 10 minutes Which of the following is CORRECT when considering the tertiary structure of globular proteins? A) B sheets are usually twisted or wrapped into barrel structures. B) Hydrophobic residues are normally on the inside and hydrophilic residues are on the outside. C) The amino acid proline never occurs in a region where the polypeptide chain bends or turns. D) All parts of the proteins can be classified as helix, ß sheet or turns. away from the Protein folding is a random process, whereby a vast number of possible conformations are tested to find the desired most stable state. A) True B) False C) Not enough information to determine D) Protein folding is completely random. 5. Protein folding is a thermodynamically favorable process under physiological conditions because A) There is an increase in entropy associated with protein folding B) There is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule C) Of the large negative enthalpy change associated with many noncovalent interactions D) No intermediate stage disulfide bonds form during the folding process B) Secondary C) Tertiary D) Quaternary structure. 6. The functional organization of proteins where specific complexes of two or more polypeptides are formed is called A) Primary
Transcribed Image Text:Name : Surname: 2. 3. 4. The amino acid side chain residues in an a helix point center of the helix. A) Outward B) Inward C) Perpendicular D) Horizontally Please I need the solution in 10 minutes Which of the following is CORRECT when considering the tertiary structure of globular proteins? A) B sheets are usually twisted or wrapped into barrel structures. B) Hydrophobic residues are normally on the inside and hydrophilic residues are on the outside. C) The amino acid proline never occurs in a region where the polypeptide chain bends or turns. D) All parts of the proteins can be classified as helix, ß sheet or turns. away from the Protein folding is a random process, whereby a vast number of possible conformations are tested to find the desired most stable state. A) True B) False C) Not enough information to determine D) Protein folding is completely random. 5. Protein folding is a thermodynamically favorable process under physiological conditions because A) There is an increase in entropy associated with protein folding B) There is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule C) Of the large negative enthalpy change associated with many noncovalent interactions D) No intermediate stage disulfide bonds form during the folding process B) Secondary C) Tertiary D) Quaternary structure. 6. The functional organization of proteins where specific complexes of two or more polypeptides are formed is called A) Primary
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