1. What is difference between affinity and avidity? 2. Does inside-out signaling
ID: 178446 • Letter: 1
Question
1. What is difference between affinity and avidity?
2. Does inside-out signaling enhance affinity, avidity, or both? Explain.
12. Which technique was utilized to demonstrate that separation of the intracellular domains of the alpha and beta chains accompanies inside-out signaling?
13. What is the role of cytoplasmic-tail binding proteins in regulating ligand binding affinity?
14. Which adhesion molecule/s facilitate/s the rolling of lymphocytes prior to diapedesis?
17. Which technique was used to identify proteins that interact with cytoplasmic domains of beta2-integrin and what is its principle?
19. Which experiments revealed the role of Rho-H in maintaining the low affinity state of integrins?
20. What is the likely role of polarized vesicular transport and LFA internalization in trafficking?
Explanation / Answer
ANSWERS:
1. Affinity is a likeliness of a ligand to bind whereas avidity is a property and measure of the cell to cell adhesiveness. Thus, the affinity is the strength of binding of one molecule to ligand and the avidity is the sum of strengths of various molecules binding to a ligand.
In immunology, an antibody reacts with an antigen by forming a reversible non-covalent bond. The kind of bond formed depends on the valency of the antibody. The strength of this complex formed between the two is described either by the affinity or the avidity.
Affinity - It is the strength of antigen-antibody complex when a single epitope present on the antibody binds to only a single antigen binding site. This interaction is very specific.
Avidity - It is the strength of antigen-Ab complex in the case of multivalent Abs. It measures the total overall strength of all interactions. Avidity depends on the affinity, valency, and arrangement of the structure.
2. During cell -cell interaction and signaling, the avidity increases due to inside-out signaling. It also has an effect on the ligand binding property by bringing about conformational changes due to which indirectly, the affinity also increases.
12. Nuclear Magnetic Resonance (NMR), FACS analysis and X-ray crystallography
13. .The role of cytoplasmic-tail binding proteins in regulating ligand binding affinity is the regulation of following steps:
14. Endothelial cellular adhesion molecules such as selectins, cadherins, and junctional adhesion molecules like the JAM-1, PECAM-1, LAF-1, CD99 etc
19. Experiments on T-cell migration revealed the role of Rho-H in maintaining the low-affinity state of integrins
20. During trafficking, the polarized vesicles Direct the delivery of proper cargo proteins to their specific destination. These proteins help in forming the basolateral domain and apical domain for determining the polarity of epithelial cell while trafficking
LAF internalization leads to the activation of integrins during trafficking.
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