生化名解英文部分.docxVIP

1 The partial double-bond character of the peptide bond makes Cα1, C, O, N, H, Cα2 six atoms coplanar, Cα1 and Cα2 are trans to each other, this semi-rigid plane composed of those six atoms is termed as peptide unit.2 Motifs are the assembling of more than 2 secondary structural elements that fold to near each other in space and have special functions.3 The tertiary structure of some proteins can be divided into two or more relatively independent compact regions that may be joined by a flexible segment of the chain, and have special functions. These compact units called domains4 Protein spatial structures are sensitive to denaturing agents (high T, urea, strong acids or bases, organic solvents, detergents, heavy metal ions)These agents result in unfolding and disorganization of protein spatial structure without change in primary structure, and associate with loss of biological activity5 pI is the pH at which protein molecular becomes electrically neutral, has no net electric chargepositive charged: pH pI negative charged: pHpI6 Secondary structures: the localized folding segments of the polypeptide backbone Common secondary structures:α-helix (α螺旋) β- pleated sheet (β折叠) random coil (无规卷曲) β –turn(bend)(β转角) Forces: hydrogen bonds1 Enzymes are highly efficient biocatalysts which are involved in almost all biological reaction. Enzymes are proteins in chemical nature. They have special conformation and can be denatured Some RNA/DNA have enzyme activity, which are called Ribozymes 2 active center, catalytic site-- Active site is a three-dimensional, local region of the enzyme, the region is composed of several essential groups of AAs, that has special spatial structure which specifically binds substrate and catalyzes it to become product-- Coenzymes or prosthetic groups can be involved in active site3 small allosteric effectors, which generally have little or no structural similarity to the substrate, binding to allosteric site of the enzyme by non-covalent