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dc.contributor.authorelMasry, Nadia Farida
dc.date.accessioned2021-11-25T15:22:25Z
dc.date.available2021-11-25T15:22:25Z
dc.date.submitted1993-07-04
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/331162
dc.description.abstractThe 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.en
dc.language.isoenen
dc.publisherDepartment of Chemistryen
dc.subjectthermodynamicsen
dc.subjectmethyleneen
dc.subjecthydrophobic coreen
dc.titleFolding Studies on Mutants of Chymotrypsin Inhibitor 2en
dc.typeThesisen
dc.type.qualificationleveldoctoralen
dc.type.qualificationnamePhDen
dc.publisher.institutionUniversity of Cambridgeen
dc.identifier.doi10.17863/CAM.78609


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