剖析第一章： 蛋白质的结构层次1.pptVIP

* Proteins – biopolymers (called polypeptides) of L-amino acids. 2. joined via peptide bonds. 3. Only L-amino acids (rare D-form) 4. Different proteins have different sequences The primary sequence determines the 3-D structure * 3, peptide bond Peptide bonds form in the process of translation when the α-amino group of one amino acid residue forms a covalent bond with the α -carboxyl group of another amino acid residue. * * Gly+Ala ? Gly-Ala (Glycylalanine) * All the atoms in such a unit are fix in a plan with the bond length And bond angles very nearly the same in all units in all proteins * the peptide bond can be considered a resonance hybrid of the forms Peptide C-N bonds are unable to rotate freely because of their partial double-bond character * Rotation around the bonds in a polypeptide chain.???? Each unit can rotate around two such bond Cα-C’and N- Cα Angle: φ, ψ Phi: the angle of rotation around the N-Cα Psi: the angle of rotation around the C’-Cα * Left: Observed values for all residue type except glycine. Right: Observed values for glycine Many values are prohibited by steric interference between atoms in the polypeptide backbone are amino acid side chain * pI: isoelectric point (Isoelectric focusing) a distinct pH at which the net average charge of all the groups adds up to zero. The relative concentrations of the three forms of glycine as a function of pH non-charged * Groups that may block N- or C-termini in proteins. * 5, protein sequencing and sequence analysis 1) Edman P. 1950: PITC (Edeman) degradation, N-terminal sequencing 2) Sanger et al. 1953, complete sequence of bovine insulin (21+30 res.) 3) amino acid sequence deduced from the open reading frame (ORF) PTIC: 苯异硫氰酸脂 * Applying MS (Mass Spectrometry) in protein sequence determination 1) partial or complete proteolysis of the target protein 2) determine the mass of all fragments (MS/MS) 3) calculate the possible sequences based on the results from 2 4) reconstruction by ov