生化填空（Biochemical filling）.docVIP

生化填空（Biochemical filling） 1. protein is an important component of the organism, and its physiological functions are as follows: some proteins are enzymes and play a catalytic role in metabolism; some proteins are hormones, which play a regulatory role in metabolism. In addition, some proteins have functions such as movement, transportation and immunity. 2., according to the polarity of R group, the 20 amino acids of proteins can be divided into 4 types: non-polar hydrophobic amino acids, polar non charged amino acids, polar negatively charged amino acids and polar positively charged amino acids. The negatively charged amino acids in PH=7 are aspartic acid and glutamic acid, and the positively charged amino acids are lysine, arginine, and histidine. 3. proteins in organisms are composed of 20 amino acids of the L- configuration. 4. amino acids are heated together with the three keto ketone to form a blue purple compound, while the reaction product of proline is yellow. 5., the peak of UV absorption of proteins is 280nm, which is caused by phenylalanine, tyrosine and tryptophan. 6. the primary structure of the protein was determined by using Sanger reagent 2,4- two, and the Edman reagent was isothiocyanate, which was determined from the N end of the peptide segment sequence. Edman reaction can analyze more than 70 amino acid residues. In the 7. protein alpha helix model, each rotation contains 3.6 amino acid residues, increasing 0.54nm, each peptide plane rotates 100 degrees along the axis, and the longitudinal axis of each amino acid residue is 0.15nm. In the 8. alpha helix model, a hydrogen bond is formed between the 5 amino acids, and a hydrogen bond is formed between the 4 amino acid residues in the beta rotation structure. The bovine insulin measured by Sanger in 9.1953 years is composed of 51 amino acid residues. There are two strands, A chain, 21 amino acid residues, B chain, 30 amino acid residues, and there are 2 S- S- bonds between A and B chains. 10., the t