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Hydrophilicity Plot is a computer plot which checks the relative summed hyrophobicity or hydrophilicity of adjacent amino acid sidechains (usually within a moving window of about 6 amino acid residues) along with the the primary sequence of a polypeptide chain. Values for contribution of sidechains of each the 20 common amino acids to hydrophobicity or hydrophilicity have been developed by Hopp & Woods, and Kyte & Doolittle, and these plots are generally named after these workers. Usually, hydrophobic regions of proteins are considered likely to be in the interior of the native protein, whereas hydrophilic domains are probable to be exposed on the surface and thus possibly antigenic sites (epitopes). At best, these are crude predictions.
Question 1 Explain how will you perform ward radiography? Question 2 Discuss the radiographic projections recommended for imaging the first to third cervical vertebr
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Define interaction of Vitamin C with Riboflavin? The two coenzyme forms of riboflavin are FMN and FAD. They are found in a large number of systems which function in the metabol
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Q What are the three structures shared by every chordate that characterize the group? All beings of the phylum Chordata have branchial clefts in the pharynx in some species pre
please give me the expansion for ''gradient hypothesis'' and the two types of gradient hypothesis in deelopment of animals in detailed manner
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Define sex
in natural vegetative propagation which structure gives rise to new individuals?
Q. What is the cellular regeneration? How is the mitosis related to this process? Some tissues are capable to regenerate when injured. The liver, for instance, regenerates when
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