The oxygen-haemoglobin dissociation curve, also spelled oxygen-hemoglobin dissociation curve, plots the proportion of hemoglobin in its saturated form on the vertical axis against the prevailing oxygen tension on the horizontal axis. The oxyhemoglobin dissociation curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO2) and partial pressure of oxygen in the blood (PO2), and is determined by what is called "hemoglobin's affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it. found on wikipedia
To calculate the dissociation constant (Kd) from a binding curve, you can determine the concentration of ligand at which half of the binding sites are occupied. This concentration is equal to the Kd value.
when we excercising, tissue generates heat.those heat would increase the temperature of the neighboring cell, that exercise and need more energy. thus, more oxygen is needed, making the graph shift to the right because hemoglobin release oxygen faster to accord the increasing demand during exercise.
Another way to describe the dissociation of water is as follows where two water molecules form a hydronium ion (essentially a water molecule with a proton attached) and a hydroxide ion
Lumbar-pelvic dissociation refers to the independent movement of the lumbar spine (lower back) and the pelvis. This separation of movement is important for functional activities such as walking, running, and bending at the waist. Insufficient lumbar-pelvic dissociation can lead to compensatory movements and potential risk for injury.
An "S' curve (on a population chart) reaches its carrying capacity and levels out, while a "J" curve hits its carrying capacity and just continues causing a population explosion and competition for resources.
To calculate the dissociation constant (Kd) from a binding curve, you can determine the concentration of ligand at which half of the binding sites are occupied. This concentration is equal to the Kd value.
change in pH , temp. carbon dioxide 2,3 BPG shifts the curve
To determine the acid dissociation constant (Ka) from a titration curve, one can identify the equivalence point on the curve where the amount of acid equals the amount of base added. By analyzing the pH at the equivalence point and using the initial concentration of the acid, the Ka can be calculated using the Henderson-Hasselbalch equation.
Paul Emerick...lol
As it shifts to the right, it means that haemoglobin has a lesser affinity for oxygen
Answering "http://wiki.answers.com/Q/Why_the_titration_curve_is_varying_with_different_acid_base_titration"
A negative feedback mechanism is a system to return a disruption in homeostasis back to homeostasis.A positive feedback mechanism is a system to reinforce or perpetuate a disruption in homeostasis.The oxyhemoglobin dissociation curve represents the Partial pressure in oxygen that will be saturated in the amount of hemoglobin.This curve represents a positive feedback because the binding of Oxygen to hemoglobin facilitates more binding of oxygen to hemoglobin (you can see this in the rapid rise in saturation from 10-40 mm Hg) until it reaches 60 mm Hg where it is somewhat completely saturated
To calculate the dissociation constant (KD) from a binding curve, you can use the equation KD C50, where C50 is the concentration of the ligand at which half of the binding sites are occupied. This value can be determined by plotting the binding data and finding the point where half of the maximum binding is achieved.
The titration curve of H3PO4 shows that it is a triprotic acid, meaning it can donate three protons (H ions) in a stepwise manner. The curve displays three distinct equivalence points, indicating the presence of three dissociation steps. This reveals that H3PO4 has multiple acidic hydrogen atoms with different strengths of acidity.
Dissociation is a dangerous mental disease.
Dissociation is an endothermic process.
To experimentally determine the dissociation constant (Kd), one can perform a series of experiments where the concentration of a ligand is varied while measuring the binding affinity to a receptor. By plotting the data and analyzing the binding curve, the Kd value can be calculated as the concentration of ligand at which half of the receptor sites are occupied.