Which set of amino acids will likely to be located on the interior of a globular protei O Lys, Phe, Asp Val, Phe, Ala O Asp, Phe, Ala O Val, Lys, Asp
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- Show where trypsin and chymotrypsin would cleave the following peptide Tyr-Ile-Gin-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gin GinSpinal fluid contains 15 to 45 mg/dL protein. If you were to take a 5.0 mL sample of spinal fluid, how much protein could you expect to find? Express your answer as a range.The following sequence of amino acids are part of adult hemoglobin from the N-terminus. Draw the skeletal structure of this peptide. Val-His-Leu-Thr-Pro-Glu-Glu-Lys-Ser-Ala-Val-Thr
- Identify the polar amino acids, the aromatic amino acids,and the sulfur-containing amino acids, given a peptide with thefollowing amino acid sequence:Val-Met-Ser-Ile-Phe-Arg-Cys-Tyr-LeuIdentify the nonpolar amino acids and the acidic aminoacids in the following peptide:Glu-Thr-Val-Asp-Ile-Ser-AlaI now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygen
- Myoglobin monomers are likely to have more hydrophilic amino acids on the protein surface than Hemoglobin monomers. True or FalseThesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portionIn myoglobin (above), which level of protein organization includes peptide bonds, hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waal forces? the primary structure the secondary structure the tertiary structure the quaternary structure all of the above
- Vasopressin is a hormone that plays an important role in social behavior, sexual motivation, and maternal responses to stress. Estimate its isoelectric point (ip) if it is known that the aminoacid sequence of vasopressin is: Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-GlyThe primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.The smooth muscle cells are arranged in two different ways in intestinal wall. Explain the significance of two different arrangements of smooth muscle cells in intestinal wall i.e. how these arrangements relate to the function.