Abstract
The partial specific volume (V) and adiabatic compressibility (β) of myoglobin have been shown to be reduced by small cosolvents such as glycerol (A. Priev, A. Almagor. S. Yedgar, B. Gavish, Biochemistry 35 (1996) 2061- 2066). To elucidate the effect of the cosolvent size on these protein properties, in the present study we determined V and β of myoglobin in solutions containing a homologous cosolvent series from sucrose to dextran - 500 (M.W. 500000). It was found that in addition to the expected effect of the cosolvent concentration, V and β decrease with increasing cosolvent M.W. This suggests that structural properties of the cosolvent contribute to its effect on the protein interior.
| Original language | English |
|---|---|
| Pages (from-to) | 151-156 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
| Volume | 1382 |
| Issue number | 1 |
| DOIs | |
| State | Published - 15 Jan 1998 |
Bibliographical note
Funding Information:This work was supported by a Grant to S. Yedgar from the USA-Israel Binational Science Foundation (91-00164).
Keywords
- Adiabatic compressibility
- Macromolecular cosolvents
- Myoglobin
- Protein specific volume
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