BB400: Molecular Biophysics

Molecular structure; Torsion angles; Steric effect: Contact distances; Homomorphous sugars; Cis & trans peptide bonds; Ramachandran map: for amino acids and as a general conformational analysis tool. Non-covalent interactions; hydrogen bond; stacking; Entropy: Entropy/enthalpy compensation; A=T vs. GÂșC. Effective conc. Enthalpic and entropic co-operativity. Oligopeptide conformation. Conformationally constrained amino acids; Hydrophobic effect; Affinity and specificity in intermolecular interactions; Stability of protein structure; Folding / unfolding; m values; Models of protein folding; Folding funnel; Contact order; F value analysis; Denatured state; Intrinsically unfolded proteins; Protein and RNA folding; In vivo folding; Kinetically stable proteins; Lipids: Assemblies; Volume, surface area, length relationship; X-ray studies; Phase transitions of anhydrous and hydrated lipid bilayers.

Text/References :

  • Biophysical Chemistry, Vol. 1 & 3. C.R.Cantor and P.R.Schimmel; W.H. Freeman, 1980.
  • Proteins. Structure and Molecular properties. T.Creighton. W.H.Freeman, 2nd ed. 1992.
  • Protein structure. A practical approach. T.Creighton. Oxford Univ. Press. 2nd ed. 1997.
  • The structure of biological membranes. P.L.Yeagle. CRC Press. 2nd ed. 2004.