I. II. III. IV. O HẲN-CH-CANH-CH,C-NH-CH-CƠ V. O CH3 alanyl 2. Types of protein structures: What is the type of protein structure that contains a single strand and bound by disulfide bond. glycyl serine OH CH, 0 TI H₂N-C-C-OH H The structure containing an alpha- helix The structure contains beta pleated sheets The structure is made up of O CH₂OH subunit What is the difference between a tertiary structure and a quaternary structure? protein structures? 3. Indicate which structure is at low pH (acidic, basic or neutral (zwitterion) H R H₂N-C-COO™ 4. What are five factors that affects 5.Indicate the amino acid as polar or nonpolar OH CH, O H₂N-C-C-OH CHÀO H₂N-C-C-O™ CH3 CH₂ C CH CH₂O 11₂N-C-C-0 H 6) Acids and bases denature a protein by disrupting A) peptide bonds and ionic bonds. B) amide bonds and alkene bonds. C) hydrophobic interactions and peptide bonds. D) ionic bonds and hydrophobic interactions. E) ionic bonds and hydrogen bonds. 5) Heat denatures a protein by disrupting A) ionic bonds and peptide bonds. B) hydrophobic bonds and hydrogen bonds. C) peptide bonds and hydrophobic bonds. D) disulfide bonds and peptide bonds. E) hydrogen bonds and disulfide bonds. 7) Denaturation of a protein A) changes the primary structure of a protein. B) disrupts the secondary, tertiary, or quaternary structure of a protein. C) is always irreversible. D) hydrolyzes peptide bonds. E) can only occur in a protein with quaternary structure. CH: 0 I -C-0 8) Heavy metals denature proteins by A) releasing amino acids. B) disrupting hydrophobic interactions. C) changing the pH of the protein solution. D) changing the temperature of the protein solution. E) disrupting disulfide bonds. 9) An acid can denature a protein. by A) agitating the protein chains. H₂N-C B) disrupting hydrogen bonds between R groups chains. H C) disrupting hydrophobic interactions within
I. II. III. IV. O HẲN-CH-CANH-CH,C-NH-CH-CƠ V. O CH3 alanyl 2. Types of protein structures: What is the type of protein structure that contains a single strand and bound by disulfide bond. glycyl serine OH CH, 0 TI H₂N-C-C-OH H The structure containing an alpha- helix The structure contains beta pleated sheets The structure is made up of O CH₂OH subunit What is the difference between a tertiary structure and a quaternary structure? protein structures? 3. Indicate which structure is at low pH (acidic, basic or neutral (zwitterion) H R H₂N-C-COO™ 4. What are five factors that affects 5.Indicate the amino acid as polar or nonpolar OH CH, O H₂N-C-C-OH CHÀO H₂N-C-C-O™ CH3 CH₂ C CH CH₂O 11₂N-C-C-0 H 6) Acids and bases denature a protein by disrupting A) peptide bonds and ionic bonds. B) amide bonds and alkene bonds. C) hydrophobic interactions and peptide bonds. D) ionic bonds and hydrophobic interactions. E) ionic bonds and hydrogen bonds. 5) Heat denatures a protein by disrupting A) ionic bonds and peptide bonds. B) hydrophobic bonds and hydrogen bonds. C) peptide bonds and hydrophobic bonds. D) disulfide bonds and peptide bonds. E) hydrogen bonds and disulfide bonds. 7) Denaturation of a protein A) changes the primary structure of a protein. B) disrupts the secondary, tertiary, or quaternary structure of a protein. C) is always irreversible. D) hydrolyzes peptide bonds. E) can only occur in a protein with quaternary structure. CH: 0 I -C-0 8) Heavy metals denature proteins by A) releasing amino acids. B) disrupting hydrophobic interactions. C) changing the pH of the protein solution. D) changing the temperature of the protein solution. E) disrupting disulfide bonds. 9) An acid can denature a protein. by A) agitating the protein chains. H₂N-C B) disrupting hydrogen bonds between R groups chains. H C) disrupting hydrophobic interactions within
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
Related questions
Question
Transcribed Image Text:**Educational Content on Protein Structure and Denaturation**
**1. Diagram Explanation**
The provided diagram shows a sequence of amino acids, specifically alanine, glycine, and serine, with their respective structures and functional groups. It visually represents the peptide bond formation between amino acids and highlights different side chains.
**2. Types of Protein Structures**
I. **Primary Structure**: A type of protein structure that contains a single strand and is bound by a disulfide bond.
II. **Secondary Structure - Alpha Helix**: The structure containing an alpha-helix.
III. **Secondary Structure - Beta Pleated Sheets**: The structure contains beta pleated sheets.
IV. **Subunit Structure**: The structure is made up of subunits.
V. **Tertiary vs. Quaternary Structure**: The difference pertains to the level of complexity and interactions between subunits.
**3. pH Indication**
Identify structures as acidic, basic, or neutral (zwitterion) based on their chemical groups.
**4. Factors Affecting Protein Structures**
Five factors that affect protein structures include:
1. pH level
2. Temperature
3. Salt concentration
4. Presence of reducing agents
5. Chemical modifications
**5. Polarity of Amino Acids**
Indicate whether the provided amino acids are polar or nonpolar based on their structures.
**6. Effects of Acids and Bases on Proteins**
Acids and bases denature a protein by disrupting ionic bonds and hydrogen bonds.
**7. Heat Denaturation**
Heat can denature a protein by disrupting hydrogen bonds and disulfide bonds.
**8. Protein Denaturation**
Denaturation of a protein:
- **B**) Disrupts the secondary, tertiary, or quaternary structure of a protein.
**9. Heavy Metal Denaturation**
Heavy metals denature proteins by disrupting disulfide bonds.
**10. Acid Denaturation**
An acid can denature a protein by disrupting hydrogen bonds between R groups.
This educational content provides an overview of protein structures, ways proteins can be denatured, and factors affecting their stability.
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 3 steps with 1 images
Recommended textbooks for you
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON