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Concept explainers
a.
To determine:
The difference between primary and secondary protein structures.
Introduction:
Proteins are formed by the sequences of amino acids and these amino acids undergo condensation reaction for the formation of protein. For performing its function, protein folds into a specific spatial arrangement driven by a number of non covalent interactions, such as ionic interactions, hydrogen bonding, hydrophobic interaction and Van der Waals forces. The range of amino acids in protein structure varies from one to several thousand.
Levels of protein structure are,
- 1. Primary structure.
- 2. Secondary structure.
- 3. Tertiary structure.
- 4. Quaternary structure.
b.
To determine:
The difference between complete and incomplete protein.
Introduction:
Proteins are formed by the sequences of amino acids and these amino acids undergo condensation reaction for the formation of protein. For performing its function, protein folds into a specific spatial arrangement driven by a number of non covalent interactions, such as ionic interactions, hydrogen bonding, hydrophobic interaction and Van der Waals forces. The range of amino acids in protein structure varies from one to several thousand.
Levels of protein structure are,
- 1. Primary structure.
- 2. Secondary structure.
- 3. Tertiary structure.
- 4. Quaternary structure.
c.
To determine:
The difference between fibrous and globular protein.
Introduction:
Proteins are formed by the sequences of amino acids and these amino acids undergo condensation reaction for the formation of protein. For performing its function, protein folds into a specific spatial arrangement driven by a number of non covalent interactions, such as ionic interactions, hydrogen bonding, hydrophobic interaction and Van der Waals forces. The range of amino acids in protein structure varies from one to several thousand.
Levels of protein structure are,
- 1. Primary structure.
- 2. Secondary structure.
- 3. Tertiary structure.
- 4. Quaternary structure.
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Chapter 10 Solutions
General, Organic, and Biological Chemistry (3rd Edition)
- 1. For the four structures provided, Please answer the following questions in the table below. a. Please draw π molecular orbital diagram (use the polygon-and-circle method if appropriate) and fill electrons in each molecular orbital b. Please indicate the number of π electrons c. Please indicate if each molecule provided is anti-aromatic, aromatic, or non- aromatic TT MO diagram Number of π e- Aromaticity Evaluation (X choose one) Non-aromatic Aromatic Anti-aromatic || ||| + IVarrow_forward1.3 grams of pottasium iodide is placed in 100 mL of o.11 mol/L lead nitrate solution. At room temperature, lead iodide has a Ksp of 4.4x10^-9. How many moles of precipitate will form?arrow_forwardQ3: Circle the molecules that are optically active: ДДДДarrow_forward
- 6. How many peaks would be observed for each of the circled protons in the compounds below? 8 pts CH3 CH3 ΤΙ A. H3C-C-C-CH3 I (₁₁ +1)= 7 H CI B. H3C-C-CI H (3+1)=4 H LIH)=2 C. (CH3CH2-C-OH H D. CH3arrow_forwardNonearrow_forwardQ1: Draw the most stable and the least stable Newman projections about the C2-C3 bond for each of the following isomers (A-C). Are the barriers to rotation identical for enantiomers A and B? How about the diastereomers (A versus C or B versus C)? H Br H Br (S) CH3 (R) CH3 H3C (S) H3C H Br Br H A C enantiomers H Br H Br (R) CH3 H3C (R) (S) CH3 H3C H Br Br H B D identicalarrow_forward
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