The molecule with higher dipole moment is COFH because the geometry of the molecule in the COF2 nearly cancel the dipolar moment of each other. To be more clear:
The dipolar moment is the vectorial sum of all bond moments in the molecule or dipolar moment of each bond. The dipolar moment of a molecule with three or more atoms is determined by bond polarity as their geometry.
COF2 has a trigonal planar structure which are symmetric. The electronegativity of oxygen is slightly different regarding fluor. So as you can see in the image, the electronic density is specially displaced to the fluor atoms, but either to the oxygen atom.
COFH has a trigonal structure but differs from COF2 because there is an hydrogen who is donating it's electronic density, so in this zone the electronic density is less than over oxygen or fluor. That makes bond angles be different between them.
Answer:
C = 0.2349 J/ (g °C)
Explanation:
Mass, m = 894.0g
Initial Temperature = −5.8°C
Final Temperature = 17.5°C
Temperature change = 17.5°C - (−5.8°C) = 23.3
Heat, H = 4.90kJ = 4900 J
Specific heat capacit, C = ?
The relationship between these quantities is given by the equation;
H = mCΔT
C = H / mΔT
C = 4900 / (894)(23.3)
C = 0.2349 J/ (g °C)
Answer:
60-20=40km west because the direction Will favour whichever direction is bigger
Answer:
Role is defined below
Explanation:
A small GTP-binding protein, is an important module of the signal transduction pathway used by growth factors to initiate cell growth and differentiation. Cellular activation with growth factors such as epidermal growth factor (EGF) induces Ras to move from an inactive state linked to GDP to an active state linked to GTP. In recent times, a mixture of genetic and biochemical studies has resulted in the elucidation of a signaling pathway that leads from growth factor receptors to Ras. After joining EGF, the EGF receptor tyrosine kinase is activated, which leads to receptor auto phosphorylation in multiple tyrosine residues. Signaling proteins with homology domains Src 2 (SH2) then bind to these phosphorylated residues in tyrosine, initiating multiple signaling cascades. Distinct of these SH2 area proteins, Grb2, exists in the cytoplasm in a preformed complex with a second protein, Son of Sevenless (Sos), which can catalyze the Ras GTP / GDP exchange. After stimulation of the growth factor, the phosphorylated EGF receptor with tyrosine binds to the Grb2 / Sos complex and translocates it to the plasma membrane. It is believed that this translocation brings Sos closer to Ras, which leads to the activation of Ras. In dissimilarity, the insulin receptor does not bind Grb2 directly, but rather induces the tyrosine phosphorylation of two proteins, the substrate-1 insulin receptor and Shc, which bind to the Grb2 / Sos complex. Once Ras is activated, a cascade of protein kinases that are important in a myriad of growth factor responses is stimulated.
