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-Structure paper
Title | Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics. |
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Journal, issue, pages | Biochemistry, Vol. 39, Page 12365-12374, Year 2000 |
Publish date | Oct 7, 1999 (structure data deposition date) |
![]() | Ratnaparkhi, G.S. / Varadarajan, R. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.25 Å |
Structure data | ![]() PDB-1d5d: ![]() PDB-1d5e: ![]() PDB-1d5h: |
Chemicals | ![]() ChemComp-SO4: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE / RNASE S MUTANT(F8M) / CAVITY S PROTEIN / S PEPTIDE / RNASE S MUTANT F8(NORLEUCINE) / RNASE S MUTANT F8A CAVITY S PROTEIN S PEPTIDE |