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Why is the side chain for valine nonpolar and the side chain for serine polar? O...
In most cases, mutations in the core of a protein that replace a smaller nonpolar side...
In most cases, mutations in the core of a protein that replace a
smaller nonpolar side chain in the wild-type (e.g., Ala, Val) with
a larger nonpolar side chain (e.g., Leu, Ile, Phe, Trp) in the
mutant, result in significant destabilization and misfolding of the
mutant. What feature of the protein core explains this observation?
Why would such a mutation prevent a protein from folding
properly?
Reset Help disulfide bridges small van der Waals contacts side chains in the protein...
Determine whether the side-chain of each of the following amino acids is polar and neutral, nonpolar,...
Determine whether the side-chain of each of the following amino acids is polar and neutral, nonpolar, basic, or acidic. Polar and neutral Nonpolar Basic Acidic hydrophobic C-coo amino acid arginine Ser NHy NHs NHİ aspartate Met
SHOW WORK 1. Why is an amino acid called an amino acid? Use the following structure...
SHOW WORK 1. Why is an amino acid called an amino acid? Use the following structure for questions 3-6. The circle contains the side chain of the amino acid Lysine (Lys). I 2 Is the side chain polar or nonpolar? 3. Is the side chain hydrophilic or hydrophobic? 4. Is the side chain acidic; basic, or neutral? 5. What is the name of the functional group in the side chain? 6 What is the strongest attractive force for the side...
Which of the following is IMPROBABLE? WHY? A hydrogen bond between the side chains of glutamate...
Which of the following is IMPROBABLE? WHY? A hydrogen bond between the side chains of glutamate with the side chain of serine An ionic bond with between the side chains of lysine and aspartate Hydrophobic interactions between the side chains of leucine and isoleucine Salt bridges between alanine and histidine A backbone hydrogen bond between C=O on one amino acid with the N-H of another amino acid 4 residues away.
True or false? True False Phenylalanine's side chain is more polar than tryptophan's or tyrosine's side chains....
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...
1. Which of the following amino acids has the most hydrophobic side chain? a). E b)....
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...
"R" group polarity nonpolar, polar, or polar with H- bonds. 1. choose any two know amino acids with similar Rf and based...
"R" group polarity nonpolar, polar, or polar with H-
bonds.
1. choose any two know amino acids with similar Rf and based on the
size and polarity of their side chains, give an explanation for why
their retention factors are similar.
2. choose any two known amino acids with very different Rf values
and based on the size and polarity of their side chains, give an
explanation for why their retention factors are dissimilar.
3. Explain why lysines Rf is...
The following is an example of an O-linked oligosaccharide chain in oligosaccharide is linked to the protein by the side-chain functional B the side-chain functional group of serine or thre...
The following is an example of an O-linked oligosaccharide chain in oligosaccharide is linked to the protein by the side-chain functional B the side-chain functional group of serine or threonine residues. Fuda2-12) Gal(β1-34)GlcNAc(B1-4) aride chain in glycoproteins. The O-linkage means the GlcNAc(a1 )-) Serine GalNAc(al>3) al(B1- 4)GIcNAc(B13) Gal(B1->4)GIcNAc(3)G1>3) Fuc(a22) Draw out this polymer from the following Fischer projections of the monosaccharide. 1) Show each monosaccharide in the Haworth projection and in the Chair conformation for the six-member rings. 2) Show...
It is not amino acids side chain The cholesterol molecules associated with the B2-adrenergic receptor orient...
It is not amino acids side chain
The cholesterol molecules associated with the B2-adrenergic receptor orient so that their lone hydroxyl is near the inner leaflet edge. This is the only atom in cholesterol with hydrogen-bonding potential. Given the consistency of this orientation, identify the hydrogen bonding partner that best explains this. Amino acids side chains of the B-2 adrenergic receptor Alcohol portion of the phosphoglyceride. Phosphate group of the phosphoglyceride. Glycerol of the phosphoglyceride. • Fatty acid acyl carbonyl...
a) which amino acid tested is most polar? b) look up the structure of the amino...
a) which amino acid tested is most polar?
b) look up the structure of the amino acids. explain why it
makes sense that the amino acid you listed is more polar than the
others?
c) what amino acids are in the fruit juice?
D. CHROMATOGRAPHY Chromatography is a general technique that is used to separate various materials. In this case, students can use the unique chemistry of the amino acid to determine its migration in a specific solvent. The solutions...
In most cases, mutations in the core of a protein that replace a
smaller nonpolar side chain in the wild-type (e.g., Ala, Val) with
a larger nonpolar side chain (e.g., Leu, Ile, Phe, Trp) in the
mutant, result in significant destabilization and misfolding of the
mutant. What feature of the protein core explains this observation?
Why would such a mutation prevent a protein from folding
properly?
Reset Help disulfide bridges small van der Waals contacts side chains in the protein...
Determine whether the side-chain of each of the following amino acids is polar and neutral, nonpolar, basic, or acidic. Polar and neutral Nonpolar Basic Acidic hydrophobic C-coo amino acid arginine Ser NHy NHs NHİ aspartate Met
SHOW WORK 1. Why is an amino acid called an amino acid? Use the following structure for questions 3-6. The circle contains the side chain of the amino acid Lysine (Lys). I 2 Is the side chain polar or nonpolar? 3. Is the side chain hydrophilic or hydrophobic? 4. Is the side chain acidic; basic, or neutral? 5. What is the name of the functional group in the side chain? 6 What is the strongest attractive force for the side...
"R" group polarity nonpolar, polar, or polar with H-
bonds.
1. choose any two know amino acids with similar Rf and based on the
size and polarity of their side chains, give an explanation for why
their retention factors are similar.
2. choose any two known amino acids with very different Rf values
and based on the size and polarity of their side chains, give an
explanation for why their retention factors are dissimilar.
3. Explain why lysines Rf is...
The following is an example of an O-linked oligosaccharide chain in oligosaccharide is linked to the protein by the side-chain functional B the side-chain functional group of serine or threonine residues. Fuda2-12) Gal(β1-34)GlcNAc(B1-4) aride chain in glycoproteins. The O-linkage means the GlcNAc(a1 )-) Serine GalNAc(al>3) al(B1- 4)GIcNAc(B13) Gal(B1->4)GIcNAc(3)G1>3) Fuc(a22) Draw out this polymer from the following Fischer projections of the monosaccharide. 1) Show each monosaccharide in the Haworth projection and in the Chair conformation for the six-member rings. 2) Show...
It is not amino acids side chain
The cholesterol molecules associated with the B2-adrenergic receptor orient so that their lone hydroxyl is near the inner leaflet edge. This is the only atom in cholesterol with hydrogen-bonding potential. Given the consistency of this orientation, identify the hydrogen bonding partner that best explains this. Amino acids side chains of the B-2 adrenergic receptor Alcohol portion of the phosphoglyceride. Phosphate group of the phosphoglyceride. Glycerol of the phosphoglyceride. • Fatty acid acyl carbonyl...
a) which amino acid tested is most polar?
b) look up the structure of the amino acids. explain why it
makes sense that the amino acid you listed is more polar than the
others?
c) what amino acids are in the fruit juice?
D. CHROMATOGRAPHY Chromatography is a general technique that is used to separate various materials. In this case, students can use the unique chemistry of the amino acid to determine its migration in a specific solvent. The solutions...
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