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PMID: 2000379 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Energetics of repacking a protein interior.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 5 ·1991-03-01 ·Pages 1706-10

Sandberg WS, Terwilliger TC

Abstract

To test whether interactions in the hydrophobic core of a protein can be adequately modeled based on the properties of a liquid hydrocarbon, we measured the unfolding free energies of the wild-type bacteriophage f1 gene V protein and 29 mutants with apolar substitutions at positions 35 and 47. Stability changes arising from identical mutations at these two buried sites are quite different, suggesting that one site is more rigid than the other. Reversals of residues at positions 35 and 47 confirm that their environments are distinct. Mutants containing weakly polar residues at these two sites suggest that the protein interior is more polar than a liquid hydrocarbon. Interactions between residues at the two sites appear to be minimal. These observations are compatible with a view of protein interiors that incorporates properties of liquid hydrocarbons but also includes polar interactions and a site-dependent "packing energy" associated with changes in internal structure.

MeSH Terms
Calorimetry Coliphages/genetics Drug Stability Escherichia coli/genetics Genes, Viral Mutagenesis, Site-Directed Protein Conformation Viral Proteins/chemistry,genetics
Chemicals
Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sandberg W S
Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
Terwilliger T C
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.5.1706
Published
1991-03-01
Pages
1706-10
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC51093
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.88.5.1706 PMC Full Text View journal details
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