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Folding Studies on Mutants of Chymotrypsin Inhibitor 2 10.17863/CAM.78609 elMasry, Nadia Farida The thermodynamics and folding kinetics of mutants at the helix N-terminus and hydrophobic core of Chymotrypsin Inhibitor 2 (CI2) have been studied. All mutants adhere to a two-state model for protein folding , and are destabilised relative to wild-type. Mutation of N-cap residue S31 to Ala or Gly destabilises CI2 by nearly 1 kcal mol-1, with respect to both wild-type and the double mutant EA33EA34. Mutation of E33 or E34 to Gin, Asp and Asn progressively destabilises the protein from 0.3 - 1. I kcal mol- 1. Deletion of one methyl(ene) group from the hydrophobic core of CI2 destabilises the protein on average by 1.3 kcal mol-1, with a strong correlation between the environment of the mutation and its effect on stability. Finally, the helix N-terminus and hydrophobic core are partially formed in the transition state of CI2, with increased exposure to solvent compared to the native state. University of Cambridge 1993-07-04 Thesis doctoral PhD en https://www.repository.cam.ac.uk/handle/1810/331162 https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/5f2b39cf-b7c3-4b87-8284-51dd44e0a1e3/download afd1abb4ad7f142cb18efaf9c4e0ac43 https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/c2e15a4b-9af1-4819-ac0b-c6b05d7b4a9f/download 87eda9de84448d1f82354d60eee3eb5f thermodynamics methylene hydrophobic core