By N. V. Bhagavan, Chung-Eun Ha
Essentials of clinical Biochemistry, moment Edition: With medical Cases is the main condensed, but unique biochemistry assessment on hand at the subject. It provides modern assurance of the basics of biochemistry, emphasizing proper physiologic and pathophysiologic biochemical thoughts.
Pivotal scientific case reports reduction in figuring out uncomplicated technological know-how within the context of analysis and therapy of human illnesses, and the textual content illuminates key themes in molecular immunology and hemostasis.
Users will locate simple and primary options that may reduction scholars and execs in biochemistry, drugs, and different healthcare disciplines. the textual content is an invaluable refresher that might support clients meet USMLE and different specialist licensing exam specifications, delivering thorough introductions, key issues, multicolored illustrations of chemical buildings and figures, fact-filled tables, and prompt analyzing lists.
- Presents crucial biochemical options in the context in their organic functions
- Contains key scientific case experiences in every one bankruptcy to reinforce figuring out of uncomplicated technology and relief in additional comprehension
- Offers educational assessment figures, flowcharts, tables and multicolored illustrations
- Includes built-in, suggested interpreting reference lists in the text
- Provides a web ancillary package deal which includes PowerPoint pictures and greater than 500 examine inquiries to relief in comprehension and USMLE examination preparation
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Additional resources for Essentials of Medical Biochemistry, Second Edition: With Clinical Cases
The β-pleated sheet occurs as a principal secondary structure in proteins found in persons with amyloidosis. The generic name β-fibrilloses has been suggested for this group of disorders. The proteins that accumulate are called amyloid and are aggregates of twisted β-pleated sheet fibrils. , immunoglobulins) on selective proteolysis and other chemical modifications. The fibrillar proteins are insoluble and relatively inert to proteolysis. Their accumulation in tissues and organs can severely disrupt normal physiological processes.
Several human proteins and enzymes are selenoproteins. Selenocysteine is located in the active sites of enzymes that participate in oxidationÀreduction reactions. These include glutathione peroxidase, thioredoxin reductase, and iodothyronine deiodinase. The incorporation of selenocysteine into the growing peptide chain occurs by a unique suppressor tRNA and a stop codon. The physiological importance of selenium as an essential trace element is exemplified in a disorder of congestive cardiomyopathy known as Keshan disease.
A left-handed α-helix is less stable than a right-handed α-helix because its carbonyl groups and the R-groups are sterically hindered. The helical structure is stabilized by intrachain hydrogen bonds involving each aNH and aCO group of every peptide bond. 6 amino acid residues per turn of the helix. 5). , collagen and elastin). Whether a polypeptide segment forms an α-helix depends on the particular R-groups of the amino acid residues. Destabilization of an α-helix may occur for a variety of reasons: electrostatic repulsion between similarly charged R-groups (Asp, Glu, His, Lys, Arg); steric interactions due to bulky substitutions on the β-carbons of neighboring residues (Ile, Thr); and formation of side-chain hydrogen or ionic bonds.