学霸归纳-蛋白质与蛋白质组.docx

蛋白质与蛋白质组 伍乘风出品 Chapter 1.Protein structure Regulation of protein function: Expression, Transportation and localization, Modification, Interaction, Degradation. Proteins generally have 50 amino acid residues. Levels of structure: Amino acid residue sequence Structural elements Specific 3-dimensional structure Arrangement of subunits in multi-subunit protein There are over 300 naturally occurring amino acids on earth, but the number of different amino acids in proteins is only 20. Classification of amino acids: Acidic: aspartate(Asp, D), glutamate(Glu, E). Basic: lysine(Lys, K), arginine(Arg, R), histidine(His, H). Aromatic: tyrosine(Tyr, Y), tryptophan(Trp, W), phenyl-alanine(Phe, F). Sulfur: cysteine(Cys, C), methionine(Met, M). Uncharged hydrophilic: serine(Ser, S), threonine(Thr, T), asparagine(Asn, N), glutamine(Glu, Q). Inactive hydrophobic: glycine(Gly, G), valine(Val, V), leucine(Leu, L), isoleucine(Ile, I). Special structure: proline(Pro,P) is often located at the turn of a peptide chain. Interaction between positive and negative R groups may form a salt bridge, which is an important stabilizing force in proteins. The synthesis of all peptide chains starts from methionine. Two additional amino acids: selenocystein(硒半胱氨酸,UGA) and pyrrolysine(吡咯赖氨酸,UAG). The unusual amino acid is specified by a canonical(标准的) stop codon. The appropriate tRNA is initially charged with serine, which is subsequently modified to selenocysteine. However, tRNA can be directly charged with pyrrolysine, which represents the first case of tRNA charging with a non-canonical amino acid. Trp, Tyr, and to a lesser exten Phe, absorb ultraviolet light, which accounts for the characteristic strong absorbance of light by proteins at a wave length of 280 nm. Nonstandard amino acid: Derived from one of the 20 standard amino acids, in a modification reaction that occurs after the standard amino acid has inserted into a protein. Three ways to obtain a peptide: Purification from tissue Genetic engin