an explanation of why oxygen binding proteins like myoglobin and hemoglobin contain heme prosthetic groups, and...

an explanation of why oxygen binding proteins like myoglobin and hemoglobin contain heme prosthetic groups, and how the protein structure surrounding the heme affects the relative affinity for oxygen vs. carbon monoxide.

Expert Solution

The binding of the oxygen molecule at the sixth coordination site of the iron ion substantially rearranges the electrons within the iron so that the ion becomes effectively smaller, allowing it to move into the plane of the

queen_honey_blossom answered 3 months ago

Hemoglobin and Myoglobin, HOW is oxygen binding regulated? what other mechanisms control oxygen binding in oxygenated...

Hemoglobin and Myoglobin, HOW is oxygen binding regulated? what other mechanisms control oxygen binding in oxygenated vs deoxygenated tissues ( lung v. exercising muscles)?

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

1. a. What are the important amino acids around heme in myoglobin/hemoglobin. b. Why is Fe...

1. a. What are the important amino acids around heme in myoglobin/hemoglobin. b. Why is Fe a +2 charge in the protein environment but able to oxidize to fe 3+ in a non-protein environment? Why is this pertinent to Oxygen binding?

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

1. a. why does myoglobin with its single prosthetic group, exhibit hyperbolic O2 binding curve? b....

1. a. why does myoglobin with its single prosthetic group, exhibit hyperbolic O2 binding curve? b. Describe O2 binding behavios of myoglobin in terms of pO2 and what does the term pO2 mean (significance)? c. Explain the structural basis for cooperative oxygen binding to hemoglobin.

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?

List positive and negative effectors for oxygen binding to hemoglobin. explain cooperative binding using hemoglobin as...

List positive and negative effectors for oxygen binding to hemoglobin. explain cooperative binding using hemoglobin as an example. Correlate the NCI involved in stabilizing Hb’s and Mb’s structures. please answer all

Describe the relationship between chemical equilibrium and the binding of hemoglobin to oxygen and explain why...

Describe the relationship between chemical equilibrium and the binding of hemoglobin to oxygen and explain why strong acids are good conductors of electricity and weak acid are not please help me and explain in detail so i can understand.( preferably give examples for both questions) thanks! :)

Describe the relationship between the partial pressure of oxygen and the binding of oxygen to hemoglobin.

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.

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