CHE 4341 Lecture Notes - Lecture 4: Energy Landscape, Protein Folding, Endoplasmic Reticulum
Document Summary
Organization of subunits in a protein w/multiple subunits (an. Subunits held together by many weak, noncovalent interactions > > subunit hydrophobic (main), ion pair, h-bond, etc. structure > except covalent bonding (eg disulfide bonding) b/t subunits very rare! Forces that hold the 4 structure together are the same as that of the 3 . Often higher order types, octahedral or tetrahedral. Defined as cn, with c for cyclical and n for # of subunits. N-fold intersect a 2-fold rotational symmetry are right angles. Disrupt interactions that stabilize tertiary structure note: some proteins can be refolded or renatured. Showed that primary structure determines tertiary structure. To catalyze formation of correct disulfide bonds. Don"t make protein fold bc they are too weak. Proteins don"t sample all possible folding conformations. Most proteins fold in less than 10 seconds. Some proteins go to a molten globule state. Energy landscape guides protein towards native structure structure. Protein samples different pathways to get to its" native.
