{"id":{"repo_id":"cambridge","oai_identifier":"oai:www.repository.cam.ac.uk:1810/331162"},"canonical_url":"https://search.dev.ndltd.org/etd/cambridge/oai:www.repository.cam.ac.uk:1810/331162","repository":{"repo_id":"cambridge","name":"Cambridge University","base_url":"https://api.repository.cam.ac.uk/server/oai/request"},"display":{"title":"Folding Studies on Mutants of Chymotrypsin Inhibitor 2","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["elMasry, Nadia Farida"],"institution":"University of Cambridge","degree_name":"PhD","degree_level":"doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1993,"date_issued":"1993-07-04","date_published":"1993-07-04","updated_at":"2026-07-22T22:24:11Z","subjects":["thermodynamics","methylene","hydrophobic core"],"languages":["en"],"rights":[],"rights_urls":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/c2e15a4b-9af1-4819-ac0b-c6b05d7b4a9f/download"],"identifier_entries":[]},"links":{"outbound_url":"https://doi.org/10.17863/CAM.78609","outbound_label":"DOI","outbound_source":"dc:identifier.doi"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["elMasry, Nadia Farida"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["1993-07-04"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cambridge"]},{"key":"dc:relation.isreferencedby.uri","label":"Dc Relation Isreferencedby URI","values":["https://www.repository.cam.ac.uk/handle/1810/331162"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["PhD"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["thermodynamics","methylene","hydrophobic core"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/c2e15a4b-9af1-4819-ac0b-c6b05d7b4a9f/download"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.doi","label":"DOI","values":["10.17863/CAM.78609"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/5f2b39cf-b7c3-4b87-8284-51dd44e0a1e3/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:format.checksum.md5","label":"Dc Format Checksum Md5","values":["afd1abb4ad7f142cb18efaf9c4e0ac43","87eda9de84448d1f82354d60eee3eb5f"]},{"key":"dc:title","label":"Title","values":["Folding Studies on Mutants of Chymotrypsin Inhibitor 2"]}]}],"canonical_facts":{"dc:creator":["elMasry, Nadia Farida"],"dc:date.issued":["1993-07-04"],"dc:description.abstract":["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."],"dc:format.checksum.md5":["afd1abb4ad7f142cb18efaf9c4e0ac43","87eda9de84448d1f82354d60eee3eb5f"],"dc:identifier.doi":["10.17863/CAM.78609"],"dc:identifier.uri":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/5f2b39cf-b7c3-4b87-8284-51dd44e0a1e3/download"],"dc:language":["en"],"dc:publisher.institution":["University of Cambridge"],"dc:relation.isreferencedby.uri":["https://www.repository.cam.ac.uk/handle/1810/331162"],"dc:rights":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/c2e15a4b-9af1-4819-ac0b-c6b05d7b4a9f/download"],"dc:subject":["thermodynamics","methylene","hydrophobic core"],"dc:title":["Folding Studies on Mutants of Chymotrypsin Inhibitor 2"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["doctoral"],"dc:type.qualificationname":["PhD"]},"updated_at":"2026-07-22T22:24:11Z"}