lly spontaneous, and occurs through noncovalent interactions. This conformation is the one with the lowest Gibbs free energy kinetically accessible to the polypeptide chain under particular conditions of pH, ionic strength, and temperature of the solvent in which the folding takes place. The rate of folding is sometimes assisted by what are known as chaperone proteins.
Hemoglobin is a protein used in the body to carry oxygen to the tissues (Devlin). It is found in red cells. Insulin is a protein which is used to control blood glucose levels. Collagen is a structural protein found widely throughout the body. Enzymes such as trypsin are protein molecules. Lipoproteins, a combination of a protein and a lipid, are an essential part of all cell membranes structurally, and as transmembrane transport systems.
2. A hydrogen bond is the attractive force between the hydrogen attracted to an electronegative atom of one molecule and an electronegative atom of another molecule (Hydrogen). The electrons are usually on oxygen, nitrogen, or fluorine, which has a negative charge. The hydrogen then has a partial positive charge. For a hydrogen bond to be possible, the electronegative atom must have one or more unshared electron pairs, as in oxygen and nitrogen, and a negative partial charge. The hydrogen, with a partial positive charge, tries to find another atom of oxygen or nitrogen with excess electrons to share and is attracted to a partial negative charge.
Ionic bonds are formed from elements with low electronegativity (almost empty outer shells) reacting with elements with high electronegativity (mostly full outer shells) (Chemical). In this case there is a complete transfer of electrons rather than the partial electron sharing
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