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Effects of dimethyl sulfoxide on subunit proteins
Annals of the New York Academy of Sciences
|January 27, 1975
Summary
Dimethyl sulfoxide (DMSO) reversibly alters protein structure at low concentrations and temperatures. Higher DMSO levels or temperatures can cause irreversible protein denaturation, impacting enzyme activity and protein interactions.
Area of Science:
- Biochemistry
- Protein Chemistry
Background:
- Dimethyl sulfoxide (DMSO) interacts with biopolymers through hydrogen bonding.
- Methyl groups in DMSO may influence hydrophobic bonding in proteins at higher concentrations.
Purpose of the Study:
- To investigate the effects of DMSO on model subunit proteins.
- To understand the relationship between DMSO concentration, temperature, and protein structural changes.
Main Methods:
- Studied the impact of varying DMSO concentrations on glutamate dehydrogenase, beta-glucuronidase, and fibrinogen.
- Assessed reversibility of DMSO-induced changes using activators and substrate levels.
- Examined DMSO's effect on thrombin-mediated fibrinogen clotting.
Main Results:
- Low DMSO concentrations (≤20%) caused reversible inactivation of glutamate dehydrogenase.
- Higher DMSO concentrations or 37°C led to irreversible inactivation of beta-glucuronidase.
- DMSO inhibited fibrinogen clotting, likely by competing for binding sites on fibrinogen.
Conclusions:
- Reversible protein structural alterations occur at low DMSO levels and temperatures.
- Irreversible protein denaturation is significant at higher temperatures and DMSO concentrations.
- DMSO's effects on protein structure involve interactions with both hydrophobic and hydrophilic groups.