What happens to the COO- terminus in oxy and deoxy Hb?
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Oxy Hb- the COO- terminus have freedom of movement
Deoxy Hb- the COO- termini participate in salt linkages, and structure is
very rigid
,What is Sickle-Cell Anemia?
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Sickled-cells become trapped in small capillaries
What is maximum velocity?
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All of the active sites are filled with substrates
What amino acids have polar, uncharged R groups?
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Serine, Threonine, Cysteine, Asparagine, and Glutamine
What does Edman Degradation do?
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It removes one amino acid at a time. The limit is 50 amino acids. After 50
amino acids, the polypeptide must be hydrolyzed into smaller fractions
, What lowers Hemoglobin's affinity for O2?
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1. Hemoglobin is pH dependent. The affinity for O2 is lowered by a high
concentration of H+
2. Hemoglobin's affinity for O2 is lowered by CO2 binding
3. Hemoglobin's affinity for O2 is lowered by BPG (2,3-
bisphosphoglycerate). BPG binds tightly to deoxy Hb
Which amino acids are likely to partcipate in the transportation of H+?
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amino acids with side groups that have pKa's close to the pH of the blood
What is an epitope or antigenic determinant?
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The actual place on the antigen to which binding occurs
What happens to Fe in deoxy Hb?
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Give this one a try later!
Oxy Hb- the COO- terminus have freedom of movement
Deoxy Hb- the COO- termini participate in salt linkages, and structure is
very rigid
,What is Sickle-Cell Anemia?
Give this one a try later!
Sickled-cells become trapped in small capillaries
What is maximum velocity?
Give this one a try later!
All of the active sites are filled with substrates
What amino acids have polar, uncharged R groups?
Give this one a try later!
Serine, Threonine, Cysteine, Asparagine, and Glutamine
What does Edman Degradation do?
Give this one a try later!
It removes one amino acid at a time. The limit is 50 amino acids. After 50
amino acids, the polypeptide must be hydrolyzed into smaller fractions
, What lowers Hemoglobin's affinity for O2?
Give this one a try later!
1. Hemoglobin is pH dependent. The affinity for O2 is lowered by a high
concentration of H+
2. Hemoglobin's affinity for O2 is lowered by CO2 binding
3. Hemoglobin's affinity for O2 is lowered by BPG (2,3-
bisphosphoglycerate). BPG binds tightly to deoxy Hb
Which amino acids are likely to partcipate in the transportation of H+?
Give this one a try later!
amino acids with side groups that have pKa's close to the pH of the blood
What is an epitope or antigenic determinant?
Give this one a try later!
The actual place on the antigen to which binding occurs
What happens to Fe in deoxy Hb?
Give this one a try later!