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Macromolecular structure • Macromolecules are held together by a variety of forces • Covalent bonds impose geometrical restrictions on molecular shape − the length of the bond has negligible variability − the angle between bonds has small variability − the dihedral angle (rotation about the bond) is least constrained • Stabilizing interactions provided by weak interactions o Noncovalent bonds (hydrogen bonds or van der Waals forces) o electrostatic attraction or repulsion o hydrophobic forces DNA DNA backbone configuration is determined by a list of torsional angles The dominant interaction is the stacking of base pairs. RNA single stranded RNA can fold into variety of structures by pairing with itself group 1 intron 88-nucleotide RNA construct with two distinct folds X-ray crystal structure of bacterial ribosome Protein structure is to large extent determined by the polypeptide backbone • peptide bond is planar • the backbone is parametrized by two dihedral angles per amino acid, φ and ψ Because of steric constraints (molecular groups bumping into each other) limited combinations of φ and ψ are possible Main secondary structures are: • • α-helix β-sheet right-handed α-helix antiparallel β-sheet