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Globular proteins
These proteins comprise more or less spherical shape (compact structure). α-helics are firmly held up by weak attractive forces of numerous types that are Hydrogen bonding, disulphide bridges, salt/ionic bridges. These are commonly soluble in water. Instances are: haemoglobin, Insulin, cytochromes, pepsin, albumins, etc.
Why a covalent bond is directional? The covalent bond is formed as a result of pairing of two electrons in the atomic orbitals of two atoms. The bond then should lie along the
Volumetric method for acids and bases - chemical methods Molecular mass of an acid can be ascertained by dissolving a known mass of the acid in water and titrating the solution
Q. Explain about Structural Isomerism? When two molecules have the same atoms but different bonds, they are called structural isomers. Thus, the variation of bond type or multi
Compound A has the molecular formula C 4 H 8 O 2 . Figure 1 gives the infrared spectra of compound A. Table gives the chemical shifts and multiplicity data of the broad-ban
The freezing point of ethylene glycol is -3.2 degree-Celcius. How many grams of ethylene glycol is required in 150 L of water to achieve such temperature?
difference b/w inductive and field effect
Q. Describe about temperature scales? The temperature of an entity explains how hot or cold the object is relative to other objects. Scientists utilize two temperature scales-t
Tetracyclines: The tetracyclines consist of hydronapht-hacene skeleton like the characteristic structural unit. The structures of tetracycline are specified as follows,
Q. Describe Molarity and Molality and what is the basic diffrence between Molarity and Molality? The concentration of a solution is usually expressed as molarity (i.e., M). The
excited state for sodium
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