What question did this study set out to answer?

Characterize the structural and conformational alterations occurring in human serum albumin upon interaction with the anionic detergent sodium decyl sulfate.

June 1, 1957Journal of the American Chemical Society

Structural Effects of the Interaction of Human Serum Albumin with Sodium Decyl Sulfate1

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Authors

GMGabor MarkusUniversity Hospitals of the Ruhr-University of Bochum FKFred KarushUniversity of Pennsylvania

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Implication

In vitro analysis demonstrates structural changes in human serum albumin induced by sodium decyl sulfate, highlighting surfactant-driven conformational unfolding.

Key Points

Characterize the structural and conformational alterations occurring in human serum albumin upon interaction with the anionic detergent sodium decyl sulfate.
Conducted in vitro physicochemical binding assays combining human serum albumin with sodium decyl sulfate.
Monitored macromolecular conformational behavior and structural transitions across detergent concentration ranges.
Sodium decyl sulfate binds directly to human serum albumin, inducing concentration-dependent alterations in the native protein structure.
Surfactant interaction drives progressive conformational rearrangements, resulting in the destabilization and unfolding of the albumin scaffold.

Cite This Study

Markus et al. (1957) studied this question.

synapsesocial.com/papers/6a952dbfc163d75667fa76b2 https://doi.org/10.1021/ja01569a073

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Implication

In vitro analysis demonstrates structural changes in human serum albumin induced by sodium decyl sulfate, highlighting surfactant-driven conformational unfolding.

Structural Effects of the Interaction of Human Serum Albumin with Sodium Decyl Sulfate1

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Member takes

Implication

Key Points

Cite This Study

Structural Effects of the Interaction of Human Serum Albumin with Sodium Decyl Sulfate1

Discussion

Member takes

Implication

Key Points

Cite This Study

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