Answer:
Hemoglobin rainier differ from normal hemoglobin with respect to oxygen affinity.
Explanation:
Hemoglobin is one of the most significant protein of Red Blood Cell containing heme(that contain Fe2+ which is coordinated with four porphyrine rings) and globin protein.
Hemoglobin exist in two state one is tensed state or deoxy hemoglobin that have less affinity for oxygen, the other state is relaxed state or oxy hemoglobin that has high affinity for oxygen.
In hemoglobin rainer the formation of new di sulfide bond prevent the formation of ion pairs that normally stabilize the T state as a result T state get unstable and this unstable T state is converted to R state to achieve the stability of hemoglobin structure.
The R or relaxed state of hemoglobin has high oxygen affinity for oxygen.
Answer:
Let's have our alleles be J = dominant, j = recessive. And for fun let's make the dominant phenotype black coat, the recessive brown coat.
Heterozygous x homozygous recessive
= Jj x jj
Punnett square:
J j
j Jj jj
j Jj jj
Genotypic ratio: 2 Jj : 2 jj, or a one-to-one ratio of Jj to jj.
Phenotypic ratio: 2 black : 2 brown, or a one-to-one ratio of black to brown.
Answer:
In Anfinsen's ribonuclease A renaturation experiment,he wanted to show that protein folding entirely resides within the amino acid sequence of protein.
Explanation:
He used ribonuclease A as a model and removed urea and 2ME from the folding solution.Under these condition, ribonuclease A regains it's biological activity.
This refolding occur in in vitro conditions.
This experiment discover an enzyme called protein disulfide isomerase(PDI) which catalyze the reduction of incorrect dissulfide bonds.This also helps in trapping protein in an incorrect conformationso that it can un fold and try agin.
This PDI plays important role in proper folding,and the active site of this enzyme have disulfide.