中山大学蛋白质组学试卷.docxVIP

I.IntroductionStructure?Building blocks——amino acids?Peptide bond and peptides?Primary structure of protein?The three-dimensional structure of proteins?Getting protein structure?Integral membrane proteins?Relationship between structure and function of proteinsFunction?Principle in general?Protein folding, misfolding and diseaseRegulation?* Expression* TransportationLocalization* Modification(Phosphorylation, glycosylation, methylation, acetylation, and ubiquitin)* Interaction* DegradationLevels of structure1°: Amino acid residue sequence2°: Structural elements3°: Specific 3-dimensional structure4°: Arrangement of subunits in multi-subunit proteinNote?? ?16% N? Met for metabolic labelling? Trp, Tyr, and to a lesser extent Phe, absorb ultraviolet light. This accounts for the characteristic strong absorbance of ? light by proteins at a wavelength of 280 nm.? Count the amino acid numbers in protein.?138???? 128???? 110? symbol?Nonstandard amino acids?(hydroxyproline,hydroxylysine)?Some additional amino acids ?selenocysteine(硒半胱氨酸)andpyrrolysine(吡咯赖氨酸)Chemical synthesis of peptides????? Liquid (Solution ) phase peptide synthesis????? Solid phase peptide synthesis（SPPS）????? Pre-treatment of amino acids????? Formation of peptide bond????? Deprotect, hydrolyze and purificationDifference between biological?and chemical synthesis of peptidesTemplateOrientation 生物NC 化学CNEfficiency (A protein with 100 amino acids : Chemical synthesis--about 4 days; Biological process--about 5 seconds in E. coli)ConditionsizeSequenceSanger 1953 胰岛素反推DNA（简并性）抗原抗体 核糖体 测mRNA测一部分比对数据库Motifs(units)structure motifs1) Helix-loop-helix2 αhelices joined by bridge?2) βhairpin2 adjacent antiparallel βstrands connected by a β-turn.3) β? α? βloopAn αhelix serves as the connection between 2 parallel βstrands.function motifs ? ?Thr-Gly-Tyr,Thr-Pro-Tyr motifDomains?1) All αdomainsrepeat of helix-loop-helix motif2) All βdomainsrepeat of βhairpin gives anti-parallel βstructures3) α/ βdomainsrepeat of β? α? βmoti