Folding Studies on Mutants of Chymotrypsin Inhibitor 2

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.

Name dc:type.qualificationname

PhD

Level dc:type.qualificationlevel

doctoral

Grantor dc:publisher.institution

University of Cambridge

Year dc:date.issued

1993

Author dc:creator

• elMasry, Nadia Farida

• thermodynamics
• methylene
• hydrophobic core

Licence

• https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/c2e15a4b-9af1-4819-ac0b-c6b05d7b4a9f/download

Language dc:language

en

DOI dc:identifier.doi

https://doi.org/10.17863/CAM.78609

OAI identifier oai:identifier

oai:www.repository.cam.ac.uk:1810/331162