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Chapter-03 Amino Acids: Structure and Properties

BOOK TITLE: Textbook of Biochemistry for Medical Students

Author
1. Vasudevan DM
2. S Sreekumari
3. Vaidyanathan Kannan
ISBN
9789350250167
DOI
10.5005/jp/books/11359_3
Edition
6/e
Publishing Year
2011
Pages
8
Author Affiliations
1. Faculty of Medicine, Amrita Vishwa Vidyapeetham, (Amrita University), Kochi, Kerala, Formerly Principal, College of Medicine, Amrita, Kerala; Formerly, Dean, Sikkim Manipal Institute of Medical Sciences, Gangtok, Sikkim, Amrita Vishwa Vidyapeetham (Deemed University), Cochin, Kerala, E-mail: dmvasudevan@aims.amrita.edu, PG Programs and Research College of Medicine, Amrita Institute of Medical Sciences, Kochi, Kerala, India, College of Medicine, Amrita Institute of Medical Sciences, Kochi, Kerala, India; Sikkim Manipal Institute of Medical Sciences, Gangtok, Sikkim, India
2. Jubilee Mission Medical College, Trissur, Kerala, Sree Gokulam Medical College and Research Foundation, Thiruvananthapuram, Kerala, India, Jubilee Mission Medical College and Research Institute, Thrissur, Kerala, India, Government Medical College, Thrissur and Thiruvananthapuram, Kerala, India; Sree Gokulam Medical College and Research Foundation, Thiruvananthapuram, Kerala, India; Jubilee Mission Medical College and Research Institute, Thrissur, Kerala, India
3. Amrita Institute of Medical Sciences, Kochi, Kerala, India, Pushpagiri Institute of Medical Sciences and Research Centre, Thiruvalla, Kerala, India, Believers Church Medical College and Hospital, Thiruvalla, Kerala, India
Chapter keywords

Abstract

Most amino acids in the body are alpha amino acids. Amino acids can be classified based on their (i) Structure (ii) Side chain characters (iii) Metabolic fate, and (iv) Nutritional requirements. In solution, amino acids exist as ‘Zwitter ions’ or ‘Ampholytes’ at their characteristic isoelectric pH (pI). In this state they carry no net charge. The Imidazolium group of Histidine has a pK of 6.1 and contributes to the buffering actions of plasma proteins and hemoglobin at the physiological pH. Glycine has no asymmetric carbon atoms and therefore has no optical activity. Alpha carboxyl group of one amino acid combines with the alpha amino group of another amino acid to form a peptide bond. A peptide bond is a partial bond and hence there is no freedom of rotation. Proteins are polymers of amino acids linked adjacently by peptide bonds.

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