Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- nyiaial liio C cysteine stop phenylalanine serine tyrosine A leucine serine stop tryptophan arginine arginine arginine arginine leucine serine stop leucine proline histidine U histidine proline proline proline leucine C A glutamine glutamine asparagine asparagine lysine lysine aspartate aspartate glutamate glutamate leucine leucine isoleucine threonine serine isoleucine threonine serine C A arginine arginine glycine glycine glycine glycine isoleucine threonine A methionine threonine valine alanine valine alanine G A valine alanine valine alanine G What would be the sequence of amino acids based on the codons found on the following MRNA? 5' AUGCCCUAUAGGUGA3' leucine - Histidine - Arginine - Valine - Cysteine-Arginine | O Tyrosine - Glysine - Isoleucine - Serine - Methionine-Stop | O Methionine - Proline - Tyrosine - Arginine-Stop O Methionine - Proline -Proline - Valine-Stop |arrow_forwardIn the following polypeptide, which amino acid would be participating in hydrogen bonding with alanine, given this sequence forms an alpha helix? Please write out the full amino acid name, not the abbreviation. Met-Ala-Leu-Glu-Lys-Thr-Leu-Valarrow_forwardNonearrow_forward
- A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin and the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn—Tyr—Asp—Met—Phe—Ala—Arg Asp—Trp—Asn—Arg Gln—Met—Tyr—Cys—Pro—Ile—Arg Gln—Cys Cyanogen bromide treatment Tyr—Cys—Pro—Ile—Arg—Asn—Tyr—Asp—Met Asp—Trp—Asn—Arg—Gln—Met Phe—Ala—Arg—Gln—Cysarrow_forwardThe folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?arrow_forwardwhats the amino acid squence for thisarrow_forward
- What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.arrow_forwardWhat is the PRIMARY STRUCTURE (amino acid sequence) of the peptide depicted below? NOTE - PROVIDE YOUR ANSWER USING SINGLE LETTER AMINO ACID CODES, without spaces between each letter. HO. OH OH -NH ОНО но. OH OH NH ENH но NH2arrow_forward
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