Exam 7: Protein Function Part I: Myoglobin and Hemoglobin

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Matching -When unstable hemoglobin is degraded;degradation products often cause cell lysis,leading to a condition called ______.

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The primary structure of mammalian hemoglobin,an α\alpha 2 β\beta 2 tetramer,is approximately _____ identical to myoglobin.

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Matching -An increase in pCO2 causes hemoglobin's affinity for oxygen to ______.

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How many antigen-binding sites are present on an IgG molecule?

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Some abnormal hemoglobins have Hill coefficients that are ______ that of normal hemoglobin,indicating that their ability to bind oxygen cooperatively has been compromised.

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Matching -The conversion of hemoglobin from the T to the R state requires breaking of ______ involving C-terminal residues.

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Which of the following statements about the symmetry model of allosterism is not true?

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How many different classes of antibodies are produced by the human immune system?

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Matching -In the ______ state of hemoglobin,the iron ion is out of the plane of the porphyrin ring.

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BPG stands for

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Matching -When oxygen binds to heme,the oxygen forms a hydrogen bond with ______.

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The oxygen binding by hemocyanins is mediated by

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Which of the statements about muscle contraction is correct?

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Which of the following increases the affinity of hemoglobin for O2?

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