Entropy is the measure of disorder in a system.

Order in a system equates to low entropy, while disorder in a system equates to high entropy. For example, for a given substance, the entropy of a gas is greater than the entropy of the liquid or of the solid. Why? The particles aren't moving around NEARLY as much in the solid or liquid as they are in the gas. They aren't as random. They are more rigid, and thus, have more order to them, and lower entropy. The negentropy, also negative entropy or syntropy [1] or extropy or entaxy, of a living system is the entropy that it exports to keep its own entropy low Small" "Middle Sized" and "Large" Biomolecules For purposes of categorizing them , divide them by size or molecular weight. The smallest ones have a molecular weight of less than 100 daltons (for example, hydrogen has a molecular weight of one dalton). The second category, the "middlesized" biomolecules, have a molecular weight between 100 and 1000 daltons the third category is of the "large" biomolecules, have a molecular weight over 1000 daltons. Both the middle-sized and macro biomolecules all contain carbon and so are called organic molecules.

8. The folded protein is a dynamic structure that can exist in different conformations with altered biological activity. 9. Many soluble, cellular proteins are globular - e.g. IgG antibodies,myoglobin, hemoglobin. 10. An IgG antibody molecule is composed of four polypeptide nchains two identical light chains, and two identical heavy chains -with two identical antigen-binding sites. 11. There are 5 different classes of H chains in antibody, each with different biological activity. 12. Myeloma proteins are homogeneous antibodies made by plasmacell tumors. 13. Collagen is the major protein of the extracellular matrix. 14. Collagen chains have an unusual amino acid composition and sequence. 15. The final functional form of a protein often involves post-translational modifications of the protein. For example, after procollagen molecules are secreted from fibroblasts, they are cleaved by specific proteases and then self-assemble into collagen fibrils. 16. Once formed, collagen fibrils are greatly strengthened by covalent cross-linking. 17. Elastin is a cross-linked, random-coil protein that gives tissues their elasticity. 18. Fibrous proteins can consist of twisted -helices (e.g. fibrin), -sheets (e.g., silk protein) or collagen triple helices. Filamentous structures can also be assembled from globular protein subunits (e.g., F-actin). 19. Proteins can have multiple conformations, some of which can induce disease states, e.g. amyloidogenic proteins and prions. 20. Prion diseases appear to be the first example of a disease caused by the transmission of a misfolded protein. Infection does not require tranmission through genetic material.

1.The amino acid sequence of a polypeptide determines its three dimensional structure in solution. 2. Noncovalent interactions are primarily responsible for maintaining protein conformation. 3. Native proteins in aqueous solutions have most of their nonpolar side chains inside, and most of their polar side chains outside. 4. Proteins contain common recurring folding patterns. 5. Many proteins contain prosthetic groups. 6. An individual protein can contain one or more subunits. 7. An alteration in a single nucleotide base coding for an amino acid in a protein can alter the function or stability of that protein causing disease.

Relationship of pK and pH to charge Every acidic or basic group on a molecule has a different pK (K is the dissociation constant) value. The relationship between the pH of the solution it is in and the pK of the ionizable group will determine the predominant form of the ionizable group. Every acidic or basic group has an acid form (also known as the protonated form) and a base form (also known as the deprotonated form). For carboxylic acids, the protonated form (acid form) is COOH and the deprotonated form (base form) is COO-. For amines, the protonated form (acid form) is NH3 + and the deprotonated form (base form) is NH2. If the pH of the solution equals the pK of the ionizable group, then the acid and base forms of that group will be present in equal amounts. If the pH of the solution is lower than the pK of the ionizable group, then the acid form of that group will be more abundant than the base form. (The predominant form is the protonated form.)

If the pH of the solution is higher than the pK of the ionizable group, then the base form of that group will be more abundant than the acid form. (The predominant form is the deprotonated form.)