Answer:
Explanation:
The switch from glutamic acid to valine in position 6 of hemoglobin (HB) forms the basis of sickle cell anemia disease pathology.
Valine is hydrophobic and it's chain is shorter than glutamic acid. The lack of the carboxylic acid and shortness of valine will result in loss of the ionic interactions formed between the glutamic acid's carboxylic group and other amino acids. A hydrophobic cavity will form in the beta sheet of HB due to the short and hydrophobic structure of valine. For these reasons, the HB molecule will be less stable and insoluble in water. The insolubility is thought to be caused by fibril formation between the valine interacting with hydrophobic pocket residues of the adjacent HB molecule. This would in turn affect binding of oxygen to HB.
For diastolic, I know the average is 120/80. Not sure about systolic
Answer:
False
Explanation:
Heat is transferred not lost
Answer:
Increasing the substrate concentration.
Explanation:
Increasing the substrate concentration can increase the rate of the reaction to a certain point. However, once all of the enzymes bounded to the substrate, any further addition of it will not be going to affect or increase the rate of the reaction at all, as all the enzymes will be saturated and working in their maximum rates.
Reproductive system and it's functions
