Myoglobin and the individual subunits of hemoglobin are similar in both size and structure. Of the...

Myoglobin and the individual subunits of hemoglobin are similar in both size and structure. Of the two, which would you predict contains a greater percentage of hydrophobic amino acids, and why?

Expert Solution

gladiator answered 1 year ago

Recognize the structure of the heme group and know its purpose in hemoglobin or myoglobin

Both myoglobin and hemoglobin exhibit cooperative binding to oxygen true or false Tropocollagen is a double...

Both myoglobin and hemoglobin exhibit cooperative binding to oxygen true or false Tropocollagen is a double helix of two left handed polypeptide chains true or false F actin is a polymer of G actin monomers and exhibits symmetry true or false Proteins have an asymmetrical tertiary structure, while multisubunit proteins can exhibit several types of symmetry true or false When referring to the amino acid sequences of proteins, sequence homology is the same as sequence similarity. true or false

Based on the structure of individual keratin subunits, why would a single point mutation in the...

Based on the structure of individual keratin subunits, why would a single point mutation in the alpha-helical region of the monomer result in a defect in the polymer? Be sure to explain it from the standpoint of DNA and intermediate filament structure.

Compare the P50 s of maternal hemoglobin, fetal hemoglobin and myoglobin. Explain why the positions of...

Compare the P50 s of maternal hemoglobin, fetal hemoglobin and myoglobin. Explain why the positions of the P50 are adaptive.

4. Based on the structure of individual keratin subunits, why would a single point mutation in...

4. Based on the structure of individual keratin subunits, why would a single point mutation in the alpha-helical region of the monomer result in a defect in the polymer? Be sure to explain it from the standpoint of DNA and intermediate filament structure.

For hemoglobin and myoglobin, discuss the mechanism, similarities, differences, and effects of O2 binding on the...

For hemoglobin and myoglobin, discuss the mechanism, similarities, differences, and effects of O2 binding on the enzymes. What happens to the enzyme structure, and what do these structural changes then cause in terms of functional changes, if any? What role does BPG play for the enzyme and why would this be the case? What about H+? How does a baby breathe in the womb?

Fetal hemoglobin consists of two alpha subunits and two gamma subunits. The gamma subunits have different residues at the 2,3-BPG binding site compared to those found in the beta subunits.

Fetal hemoglobin consists of two alpha subunits and two gamma subunits. The gamma subunits have different residues at the 2,3-BPG binding site compared to those found in the beta subunits. The charge characteristics of the different residues that are found in the gamma subunits allow for weaker binding to 2,3-BPG versus that seen in the case of adult hemoglobin, which contains two alpha subunits and two beta subunits. The statement is false. The statement is true.

The subunits of hemoglobin are arranged in a tetrahedral array with a tight spherical overall appearance...

The subunits of hemoglobin are arranged in a tetrahedral array with a tight spherical overall appearance and each individual polypeptide is folded in such a manner to maximize ____________ residues being on the exposed surface and __________ interactions being internal, making this large protein water soluble.

Explain, how following conditions influence affinity of hemoglobin and myoglobin to oxygen: a) falling of pH...

Explain, how following conditions influence affinity of hemoglobin and myoglobin to oxygen: a) falling of pH in blood plasma from pH=7.4 to pH=7.2. b) falling of partial pressure of CO2 from 6 kPa to 2 kPa c) Increase in BPG level from 5 mM to 8 mM.

describe the actuve location (S) of hemoglobin and myoglobin. How does the former function to transport...

describe the actuve location (S) of hemoglobin and myoglobin. How does the former function to transport 02 from the lungs to the cells where it is used?

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