(a)
To explain: The sign of
Introduction: Proteins are one of the most important parts of the living world. Amino acids combine to form different types of proteins. Proteins can be found in three (or four sometimes) structural forms in nature: primary structure; secondary structure; tertiary structure; and quaternary structure. Tertiary and quaternary structures are the functional structures of proteins. Simpler structures combine and fold in a special manner to form the functional proteins. The unfavorable atmosphere around the proteins can lead to the denaturation of the protein.
(b)
To explain: The sign of
Introduction: Proteins are one of the most important parts of the living world. Amino acids combine to form different types of proteins. Proteins can be found in three (or four sometimes) structural forms in nature: primary structure; secondary structure; tertiary structure; and quaternary structure. Tertiary and quaternary structures are the functional structures of proteins. Simpler structures combine and fold in a special manner to form the functional proteins. The unfavorable atmosphere around the proteins can lead to the denaturation of the protein.
(c)
To explain: Whether the contribution of
Introduction: Proteins are one of the most important parts of the living world. Amino acids combine to form different types of proteins. Proteins can be found in three (or four sometimes) structural forms in nature: primary structure; secondary structure; tertiary structure; and quaternary structure. Tertiary and quaternary structures are the functional structures of proteins. Simpler structures combine and fold in a special manner to form the functional proteins. The unfavorable atmosphere around the proteins can lead to the denaturation of the protein.
(d)
To explain: The types of bonds needed to be broken for the unfolding of a protein and why extreme heat and pH causes unfolding of the protein.
Introduction: Proteins are one of the most important parts of the living world. Amino acids combine to form different types of proteins. Proteins can be found in three (or four sometimes) structural forms in nature: primary structure; secondary structure; tertiary structure; and quaternary structure. Tertiary and quaternary structures are the functional structures of proteins. Simpler structures combine and fold in a special manner to form the functional proteins. The unfavorable atmosphere around the proteins can lead to the denaturation of the protein.
Want to see the full answer?
Check out a sample textbook solutionChapter 5 Solutions
Becker's World of the Cell (9th Edition)
- Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.arrow_forwardkcat = ? an enzyme has an aspartic acid in the active site with a pKa = 4.0 and the kcat for this enzyme is directly proportional to the fraction of this side chain that is ionized. If the kcat at pH = 4.0 is 52.9x103 s-1 what is the kcat for this enzymes at pH 3.5arrow_forwardBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : In human beings, what is the major control of de novo pyrimidine nucleotide synthesis? A. substrate availability B. competitive inhibition of carbamoyl phosphate synthetase II C. feedback inhibition of glutamine-PRPP amidotransferase D. vailability of N-acetyl glutamatearrow_forward
- Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!arrow_forwardExponential expansion? Compare the amount of information inherent in the genome, the proteome, and the glycome.arrow_forwardSerine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surelyarrow_forward
- Straight or with a twist? Account for the different structures of glycogen and cellulose.arrow_forwardIn α-helices - what is the length of the hydrogen bonds between: TYR41H and GLU37O ALA39H and MET35O GLU38H and ILE34O THR36H and ARG32O. ARG32H and TYR28Oarrow_forwardBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the transition state of a catalyzed reaction? A. higher in energy than that of an uncatalyzed reaction B. lower in energy than that of an uncatalyzed reaction C. bound very weakly to the catalyst D. lower energy than the reaction substratearrow_forward
- Color Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean protein 1ml of water and 0.5 g of glutenarrow_forwardActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartatearrow_forwardProtein folding with PDI and Peptidyl-prolyl isomerasearrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning