Question: Describe how a single amino acid substitution causes hemoglobin molecules to stick together. Use what you know about the structure of Hb and HbS, the properties of glutamic acid and valine, and how hydrophobicity causes molecules to behave in water.
Answer:
A Single amino acid must be polar to attract, just like water.
Explanation:
Sickle cell is an genetic illness and it is began by a alteration that arises in the beta sub units of the haemoglobin. Haemoglobin is a tetrameric protein made up of 2 alpha sub units and 2 beta sub units and it is the important part of the blood accountable for oxygen passage. Sickle cell is a illness that consequences from a replacement of a polar amino acid identified as glutamate with a non polar one valine at site six of the beta polypeptide component of haemoglobin. The replacement occurs as a consequence of a alteration in one of the bases in the beta-globin gene from adenine to thymine . As a outcome of this change, the beta polypeptide chains convert sticky in low oxygen circumstances since the valine sticks out of the chain and interrelates with neighboring non-polar amino acids.
Macrominerals and trace minerals.
B, immense pressure causes the core to be very compacted and solid.
Answer:
it causes the depolarization of the target cell
Explanation:
Glutamate is an excitatory amino acid neurotransmitter that binds to specific receptors on the surface of target cells and thus causes its depolarization. During glutamate-mediated depolarization, the difference in charge inside and outside the cell is lost due to the entry of sodium and calcium positive ions into the postsynaptic cell (neuron) through specific ion channels. Moreover, glutamate binding also leads to the exit of potassium ions from the cell, thereby resulting in excitation. Through this mechanism, glutamate regulates many signaling pathways, such as those involved in memory, learning, emotions, cognition, motor control, etc.
The largest energy component comes from the fats in bacon and fried eggs.
