By David M. Kaplan
Excellent for professors who are looking to supply a complete set of crucial readings within the philosophy of know-how, from foundational to the innovative, this publication introduces scholars to some of the ways that societies, applied sciences, and environments form each other. The readings learn the character of know-how in addition to the consequences of applied sciences upon human wisdom, actions, societies, and environments. scholars will learn how to get pleasure from the ways in which philosophy informs our knowing of expertise, and to determine how know-how pertains to ethics, politics, nature, human nature, desktops, technological know-how, nutrition, and animals
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Additional info for Readings in the Philosophy of Technology (2nd Edition)
E. Role of chaperones in protein folding The information needed for correct protein folding is contained in the primary structure of the polypeptide. However, most proteins when denatured do not resume their native conformations even under favorable environmental conditions. This is because, for many proteins, folding is a facilitated process that requires a specialized group of proteins, referred to as “molecular chaperones,” and adenosine triphosphate hydrolysis. The chaperones, also known as “heat shock proteins” (Hsp), interact with a polypeptide at various stages during the folding process.
Peptide bond In proteins, amino acids are joined covalently by peptide bonds, which are amide linkages between the α-carboxyl group of one amino acid and the α-amino group of another. 2). Peptide bonds are resistant to conditions that denature proteins, such as heating and high concentrations of urea (see p. 20). Prolonged exposure to a strong acid or base at elevated temperatures is required to break these bonds nonenzymically. 1 Four hierarchies of protein structure. 1. Naming the peptide: By convention, the free amino end (N-terminal) of the peptide chain is written to the left and the free carboxyl end (C-terminal) to the right.
11). This reduced affinity enables hemoglobin to release oxygen efficiently at the partial pressures found in the tissues. 10 Binding of 2,3-bisphosphoglycerate (2,3-BPG) by deoxyhemoglobin.