Which of the following are important factors in the folding of globular proteins in the cytosol? Select as many as apply. Non-polar side chains are normally found on the exterior of proteins Proteins are hydrophobic polymers The cytosol is an aqueous environment. Non-polar side chains tend to group together away from water Proteins are composed of nucleotides Proteins contain both polar and non-polar side chains Peptide bonds are very weak and easily broken

Which of the following are important factors in the folding of globular proteins in the cytosol? Select as many as apply. Non-polar side chains are normally found on the exterior of proteins Proteins are hydrophobic polymers The cytosol is an aqueous environment. Non-polar side chains tend to group together away from water Proteins are composed of nucleotides Proteins contain both polar and non-polar side chains Peptide bonds are very weak and easily broken

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter3: Cell Structure

Section: Chapter Questions

Problem 7SQ

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In a lipid bilayer, the of all the lipid molecules are sandwiched between all of the __________. a. hydrophilic tails; hydrophobic heads b. hydrophilic heads; hydrophilic tails c. hydrophobic tails; hydrophilic heads d. hydrophobic heads; hydrophilic tails
Which of the following is an example of a macromolecular assembly in a typical eukaryotic cell?* OGlycogen O Alpha globin O DNA Nucleosome Hydrophobic interactions between molecules in the cytoplasm are crucial because O They provide the necessary atoms in reactions O They facilitate the proper conformation of molecules O They allow covalent bond formation among reactants They direct the rate of chemical reactions in cells Which pair correctly depicts the relative rate at which cellular responses are generated during cellular communication? * O Altered enzyme production - fast O Altered protein synthesis - fast O Altered cell movement - slow Altered gene expression - slow
Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? O Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure O Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bonds
Which statement about N-linked glycosylation is correct? N-linked oligosaccharides are attached to proteins one sugar at the time in the endoplasmicreticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation in the endoplasmic reticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation inthe cytoplasm. N-linked sugars are attached to proteins as a 14 residue oligosaccharide after translation inthe Golgi apparatus.
Why do glycolipids exist almost exclusively on the exterior side, but not on the cytoplasmic side of the cell membrane? Flippase move the glycolipids to this side of the membrane. The inner layer of the membrane is not thick enough to accommodate carbohydrates. Carbohydrates are only added to lipids on the lumen side of the ER and Golgi membranes. Carbohydrates are removed from the cytoplasmic side by glycosylase enzymes. Next
Protein modifications that involve disulfide bonds occur in the following;(there may be more than one answer) golgi endoplasmic reticulum ) chloroplast (plastids) peroxisome mitochondria
There is a "primary driving force" behind protein folding (to form tertiary structure). This driving force can be used to explain below phenomenon except: water has a high density and a high boiling temperature non-polar amino acids go inside a protein long chain fatty acids form micelles oil spills go to the surface of water phospholipids form lipid bilayer
Which one of the these primary protein structures is most likely to form an alpha helix that would would cross a plasma membrane from the extracellular side to the cytoplasmic side? The N terminus is outside the cell and the C terminus is inside the cell in this example. Use the diagram provided to decode the one letter amino acid abbreviations. Nonpolar side chains No charged or electro- negative atoms to form hydrogen bonds; not soluble in water Polar side chains Partial charges can form hydrogen bonds; soluble in water Electrically charged side chains Charged side chains form hydrogen bonds; highly soluble in water H H₂N-C-C H₂N-C- H₂N+ Glycine (G) Gly H H H₂N* Methionine (M) Met C 8*CH₂ 6 OH 2011 Pearson Education, Inc. CH₂ CH₂ S CH₂ =0 Serine (S) Ser c=0 O O Aspartate (D) Asp 20 H₂N-C- с CH₂ H₂N* HO Acidic Alanine (A) Ala H L CH C H₂N-C C CH₂ CH₂ Threonine (T Thr H₂N C Phenylalanine (F) Phe O 0=0 CH₂ CH₂ Glutamate (E) Glu ON-DTNLRRSIAGLLIRHKKE - COOH H₂N+…
Gram-positive eubacterial cells (like Clostridium perfringens) contain which components? a cell wall made of pseudomurein, and membrane fatty acids ester-linked to glycerol (G-3-P lipids) a cell wall made of peptidoglycan, and membrane alcohols ether-linked to glycerol (G-1-P lipids) a cell wall made of cellulose, and membrane alcohols ether-linked to glycerol (G-1-P lipids) a cell wall made of pseudomurein, and membrane alcohols ether-linked to glycerol (G-1-P lipids) a cell wall made of peptidoglycan, and membrane fatty acids ester-linked to glycerol (G-3-P lipids)
Which of the following statements about glycosylation is true? the oligosaccharide on a protein leaving the ER usually is the same as an oligosaccharide transferred to that protein from dolichol the oligosaccharide transferred from dolichol is composed only of mannose glycosylation can occurs before the protein has finished its entry into the endoplasmic reticulum O cytosolic proteins are never glycosylated
A membrane-spanning protein segment has to adopt a regular secondary structure, because— Secondary structures facilitate the aggregation of nonpolar groups to increase stability. The hydrogen–bonding requirements of the polypeptide backbone have to be satisfied. α helix and β sheet have dimensions perfectly fit into the space created by the lipids. The regular structural features make it easy to align with lipid molecules in the membrane. Secondary structures can be packed tightly to minimize the surface areas.
thick layer of peptidoglycan outside of a single lipid bilayer The cell walls of Gram-negative bactena such as E. coli have a structure characterized by: proteoglycans located exterior to a lipid bilayer membrane carbohydrates that include celnulose as a major component two lipid bilayers separated by a thin layer of peptidoglycan proteins such as versican and serglycin located in the extracellular matrix b)