protein structure

Pri
1. peptide bond: 2 resonance *trans *6% Pro in Cis
  1. CN Phi; CC Psi *180 same plane *0 wont work
    1. Ramachandran plot *pics glycine
Sec
1. H bond alpha helix
  1. side chains, +/-, Asn Gln, Ser, Thr, Leu distabl; Pro: kink, N no H bond; Gly too much
  2. Stable: Ion pairs, 3/2, hydrophobic interactions aromatic
    1. every C=O NH (the 4th NH), n+4
      1. 3.5aa, 5.4 A
    2. amphipathic helix polar/non polar aa
2. Beta strand
  1. right hand, antipara, L-aa, 7 A: /\, no Pro: Phi angle, H bond
3. beta0turns
  2. 180, 4aa, H2O, near surface,
AA
1. nonpolar: G, A, P , V, L, I, M
2. polar, uncharged, S, T, C, N, Q
Tertiary
1. Globular, fibrous, membrane
  1. Globular, spherical, globular, motifs, domains, 1300
    1. helix turn helix, dimer,
    2. haripin beta (anti), b-a-b (para), greek key (4 adjacent anti b strand)
    3. b-barrels
    4. Domains
      1. distinc functions
      2. Metals, sys, His, Asp, Glu, coordinate covalent bond
        Zinc finger
      3. loops, contain aa responsible for catalytic activity
2. conformation changes, ligand binds
  1. homologs, orthologs, paralogs, superfamily
  2. sequence alignment
3. fibrous proteins, a-kertain,
Quanternary structure
1. multisubunit proteins,
  1. non-covalent ,
Protein purification L6
1. solubility
2. size, shape,
3. charge
4. binding to small molecules

Resource summary

	Created by thejoyceji about 10 years ago