生物化学期末总复习资料(双语).docVIP

生物化学复习资料 Amino acid（氨基酸）: All proteins are made up from the same set of 20 standard amino acids. A typical amino acid has a primary amino group, a carboxyl group, a hydrogen atom and a side-chain(R group) attached to a central α-group atom(Cα). Proline（脯氨酸） is the exception to the rule in that it has a secondary amino group. Primary structure（一级结构）: The linear（线状的） sequence of amino acids joined together by peptide bonds is termed（被称为） the primary structure of the protein. The position of covalent disulfide bonds between cysteine（半胱氨酸）residues is also included in the primary structure. Secondary structure（二级结构）: Secondary structure is a protein refers to the regular folding of regions of the polypeptide chain. The two most common types of secondary structure are the αhelix and βpleated sheet（β折叠）. Tertiary structure（三级结构）: Tertiary structure in a protein refers to the three-dimensional（三维的） arrangement of all the amino acids in the polypeptide chain. This biologically active, native conformation（构造；形态） is maintained by multiple（多重的；多样的） noncovalent （非共价的）bonds. Quaternary structure（四级结构）: if a protein is made up of more than one polypeptide chain it is said to have quaternary structure. This refers to the spatial（空间的） arrangement of the polypeptide subunits（亚基；亚单位） and the nature of the interactions between them. Protein stability（蛋白质稳定性）: In addition to the peptide bonds between individual amino acid residues, the three-dimensional structure of a protein is maintained by a combination of noncovalent interactions(electrostatic forces（静电力）, van derWaals forces（范德华力）,hydrogen bonds（氢键）, hydrophobic forces（疏水作用力）) and covalent interactions(disulfide bonds（二硫键）). The Bohr effect(波尔效应): H+, CO2 and 2,3-bisphosphoglycerate（2,3-二磷酸甘油酸） are allosteric effectors（变构效应剂）, promoting the release of O2 from hemoglobin（血红蛋白）. H+ and CO2 bind to different parts of the polypeptide chains, while 2,3-bisphosphoglycerate binds in the central cavity（凹穴） between the four subunits. Dialys