Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be substituted by N without affecting the conformation? b) Which residue(s) can be substituted by D without affecting the conformation? c) Which residue(s) cannot be substituted without affecting the conformation?
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Chemistry
Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be substituted by N without affecting the conformation? b) Which residue(s) can be substituted by D without affecting the conformation? c) Which residue(s) cannot be substituted without affecting the conformation?
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- LLNSAMSRLYSLRSS 1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6? 2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein? 3. at ph7 which amino acid side chain can form ionic bonds.Draw the structure of 2 five-mers (draw backbones with side chains shown as R groups) forming a beta sheetwith two anti-parallel beta strands. Indicate the hydrogen bonds present inthissecondary structure.Biochemistry: what does this picture indicate? what is difference bewteen A, B, and C ? why is it important?
- Parallel beta sheets are less stable than antiparallel beta sheets, becasue they have __________ hyrdogen bond. Fill in the blank less or more?Apamine is a small protein toxin present in the venom of the honeybee. Ithas the sequenceCNCKAPETALCARRCQQH(a) If apamine does not react with iodoacetate (see Tools of Biochemistry5B), then how many disulfide bonds are present?(b) If trypsin cleavage gave two peptides, then where is(are) the S¬Sbond(s)?Explain the role of hydrophobic exclusion during protein folding (tertiary structure); what type of aminoacids would you find towards the center of the protein? Charged? Polar? Non-polar
- Chemistry explain how the change is chemical character that occurs with the missense mutation will influence the tertiary or quaternary structure of the protein (FGFR3). How will the change in shape cause LOF or GOF. be specific! amino acid in missense mutation= S249C serine: polar uncharged, phosphorylated cysteine: nonpolar or polar, disulfide bondMost proteins denature at high temperatures. A. Are peptide bonds typically broken at high temperatures, yes or no? _________________ B. Does denaturation disrupt the primary structure of a protein, yes or no? __________________ C. Why do proteins denature at high temperatures? D. Is it likely that a denatured protein is able to perform its physiological function, yes or no? Why or why not? Thoughtfully defend your answer.Proteins treated with proteolytic enzymes hydrolyzed peptide bonds to yield a mixture of amino acids only. Is the statement TRUE OR FALSE?
- Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – CtermWhat is amphoterism? Show using chemical equations the amphoteric property of protein.BIOCHEMISTRY If the protein is more hydrophobic, then adding additional charge is not the best strategy. What are other excipients we might select instead of NaCl to try to interrupt these interactions?