Ans.) The stability of polar charged amino acids and polar uncharged amino acid are maintained by type of inter molecular bond it forms.
Polar charged molecules forms ionic bond by transfer of electrons from negatively charged to positive charged amino acid. While uncharged polar molecules forms H-bond to stabilize protein structure.
Even though hydrophobic amino acids tend to be buried in the interior of a globular protein,...
Lumpur QUESTION 2 Myoglobin is a globular protein. About half of its 153 amino acids have nonpolar side chains. Where would you expect those amino acids to be located in the tertiary structure? Inside the compact tertiary structure Outside the compact tertiary structure Evenly distrubuted On the edges of the amino acids primary chain QUESTION 3 What type of bonding is responsible for the primary structure of a protein? covalent bonds hydrogen bonds ionic bonds alpha helices
Name and draw two amino acids, one that is a hydrogen bond donor as a side chain and one that is hydrogen bond acceptor as a side chain.
True or false? True False Phenylalanine's side chain is more polar than tryptophan's or tyrosine's side chains. True False Almost all peptide bonds in proteins are in the trans configuration. True False In folded globular proteins, the side chains of hydrophobic amino acids are mostly buried in the interior of the protein. True False The peptides I-A-G-Y-L-S and S-L-Y-G-A-I are different molecules with different properties. True False Poly lysine will tend to form an alpha helix in solution at pH 6.8. True False Amyloidoses such as...
60) Lipids are composed of: c) fatty acids and glycerol amino acids and glycerol nucleic acids and glycerol fatty acids and water fatty acids and sugar e) 61) The bond between two amino acids is a: a) hydrogen bond b) covalent bond c) peptide bond d) b and c e) none of the above 62) Hemoglobin has which tertiary structure: a) fibrous b) globular c) four subunits--two alpha chains, two beta chains d) alpha helix e) none of the above...
10. A mutation in the DNA that codes for a protein has caused an amino acid with a polar charged side chain to be replaced with one that has a polar uncharged side chain. What effect should this have? More likely to be hydrophobic More likely to form an ionic bond More likely to form hydrogen bonds More likely to form disulfide bridges
Answer the following questions based upon a tripeptide sequence with the following amino acids: S L D Serine Leucine Aspartate a) What is the overall charge of the most abundant tripeptide species at neutral pH (pH 7.0)? b) At physiological pH, what is the best desciption of the chemical properties of the side chain of each amino acid? options are: hydrophobic, polar uncharged, negativelly charged, and positively charged c) What is the overall charge of the most abundant tripeptide...
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative polarity of their side chain. Consider a folded protein in an aqueous environment; where would the hydrophobic amino acids likely be found? -Tucked away in the middle of the folded protein -Randomly distributed throughout the protein -Exposed on the exterior surface of the folded protein 2. All proteins exhibit a primary, secondary, and tertiary structure, but not all proteins exhibit a quaternary structure. Describe...
Which sequence of amino acids would likely be found in the interior of a globular protein? GMWS IEDP HEKR DEAR Which of the following reactions is spontaneous in the forward direction when the reactants are my present in equirnolar amounts ? Glyceraldehyde 3 phosphate e Dihydroxyacetone phosphate creatine phosphate . ADP ATP creatine ADP. 1,3 bisphosphoglycerate 3 phosphoglycerate + ATP glycerol 3-phosphate + ADP = ATP glycerol NADH+ + H+ oxaloacetate NAD+ + malate NAD+ + pyruvate + COA NADH...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and collagen. c)are usually water soluble. d)aggregate in aqueous media. e)are often made of β-pleated sheet and α-helix sections wrapped into compact structures. 2) Select all that apply. The Bohr effect: a)depends on the atomic orbital structure of hydrogen. b)can be summarized as a reduction in the oxygen affinity of hemoglobin with decreasing pH. c)is explained by the protonation of key amino acids, including the...
1. Which of the following amino acids has the most hydrophobic side chain? a). E b). F c). S d). W e). Y 2. Which type of non covalent interaction would you expect to be present between Cl- and H2O? a). Ionic interactions ("salt links") b). Hydrogen bonds c). Van der Waals interactions d). Ion-dipole interactions For the first question, I have F and W both being hydrophobic chains but am unsure why or how to tell which one would...