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Chapter-52 Tissue Proteins in Health and Disease

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_52
Edition
6/e
Publishing Year
2011
Pages
11
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

Collagen has a triple helical structure, where the 3 strands are hydrogen bonded to each other and further stabilized by hydrogen bonds between OH groups and water molecules, thus giving high tensile strength to the fiber. Tropocollagen molecules are arranged in a quarter staggered arrays. The strength of collagen fibers is due to covalent cross-links between lysine and hydroxy lysine residues. These are formed by lysyl oxidase, which is a Cu containing enzyme. Abnormalities of collagen structure are seen in osteogenesis imperfecta, homocystinuria, Marfan’s syndrome, ascorbic acid deficiency and copper deficiency. Myosin molecules act as ATPase and binds to actin. Actin is the major protein of the thin filament. Muscle contraction is effected by the sliding of actin over myosin. Prions are proteinaceous infective particles. Prion particles (PrP) undergo change in the structural conformation and result in PrPsc. PrPsc is resistant to heat and proteolysis. Human Prion diseases are Kuru, CJD, GSSD an FFI. In animals prions can cause scrapie, BSE, nvCJD.

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