**Core Concept**
Fetal hemoglobin (HbF) is a crucial adaptation in the fetus to ensure adequate oxygen delivery from the mother's bloodstream. It has distinct properties compared to adult hemoglobin (HbA), influencing oxygen binding and release.

**Why the Correct Answer is Right**
The O2 dissociation curve of HbF is shifted to the left, indicating a higher affinity for oxygen compared to HbA. This is due to the substitution of glutamic acid with valine at position 26 (E6V) in the beta-globin chain of HbF, which reduces the oxygen affinity of the hemoglobin. As a result, HbF binds oxygen more tightly, allowing it to pick up oxygen from the mother's blood and transport it to the fetus. The leftward shift of the O2 dissociation curve ensures that HbF releases oxygen to the fetal tissues only when the partial pressure of oxygen (pO2) is low, thus facilitating oxygen delivery to the fetus.

**Why Each Wrong Option is Incorrect**
**Option A:** Incorrect - Fetal hemoglobin does not have a higher oxygen affinity than adult hemoglobin; rather, it has a higher affinity due to its unique properties.
**Option B:** Incorrect - The Bohr effect is related to the decrease in oxygen affinity of hemoglobin in response to increased CO2 and decreased pH, which is not relevant to the properties of fetal hemoglobin.

**Clinical Pearl / High-Yield Fact**
Fetal hemoglobin has a higher affinity for oxygen than adult hemoglobin, allowing it to pick up oxygen from the mother's blood and transport it to the fetus. This adaptation is crucial for fetal development and growth.

**Correct Answer: C. The O2 dissociation curve of HbF is shifted to the left, indicating a higher affinity for oxygen compared to HbA.**