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Native-state interconversion of a metamorphic protein requires global unfolding. Biochemistry 2011 Aug 23;50(33):7077-9

Date

07/23/2011

Pubmed ID

21776971

Pubmed Central ID

PMC3160782

DOI

10.1021/bi200750k

Scopus ID

2-s2.0-80051739153   22 Citations

Abstract

Lymphotactin (Ltn) is a unique chemokine that under physiological solution conditions displays large-scale structural heterogeneity, defining a new category of "metamorphic proteins". Previous Ltn studies have indicated that each form is required for proper function, but the mechanism of interconversion remains unknown. Here we have investigated the temperature dependence of kinetic rates associated with interconversion and unfolding by stopped-flow fluorescence to determine transition-state free energies. Comparisons of derived thermodynamic parameters revealed striking similarities between interconversion and protein unfolding. We conclude that Ltn native-state rearrangement proceeds by way of a large-scale unfolding process rather than a unique intermediate structure.

Author List

Tyler RC, Murray NJ, Peterson FC, Volkman BF

Authors

Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Chemokines, C
Humans
Kinetics
Models, Molecular
Protein Conformation
Protein Unfolding
Temperature
Thermodynamics
jenkins-FCD Prod-461 7d7c6113fc1a2757d2947d29fae5861c878125ab