Abstract
This article describes a combined experimental, theoretical, and computational effort to show how the complexity of aqueous hydration can influence the structure, folding and aggregation, and stability of model protein systems. The unification of the theoretical and experimental work is the development or discovery of effective amino acid interactions that implicitly include the effects of aqueous solvent. We show that consideration of the full range of complexity of aqueous hydration forces such as many-body effects, long-ranged character of aqueous solvation, and the assumptions made about the degree of protein hydrophobicity can directly impact the observed structure, folding, and stability of model protein systems.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5424-5426 |
| Number of pages | 3 |
| Journal | Journal of Physical Chemistry B |
| Volume | 103 |
| Issue number | 26 |
| State | Published - Jul 1 1999 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
Cite this
Determining the role of hydration forces in protein folding. / Sorenson, Jon M.; Hura, Greg; Soper, Alan K.; Pertsemlidis, Alexander; Head-Gordon, Teresa.
In: Journal of Physical Chemistry B, Vol. 103, No. 26, 01.07.1999, p. 5424-5426.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Determining the role of hydration forces in protein folding
AU - Sorenson, Jon M.
AU - Hura, Greg
AU - Soper, Alan K.
AU - Pertsemlidis, Alexander
AU - Head-Gordon, Teresa
PY - 1999/7/1
Y1 - 1999/7/1
N2 - This article describes a combined experimental, theoretical, and computational effort to show how the complexity of aqueous hydration can influence the structure, folding and aggregation, and stability of model protein systems. The unification of the theoretical and experimental work is the development or discovery of effective amino acid interactions that implicitly include the effects of aqueous solvent. We show that consideration of the full range of complexity of aqueous hydration forces such as many-body effects, long-ranged character of aqueous solvation, and the assumptions made about the degree of protein hydrophobicity can directly impact the observed structure, folding, and stability of model protein systems.
AB - This article describes a combined experimental, theoretical, and computational effort to show how the complexity of aqueous hydration can influence the structure, folding and aggregation, and stability of model protein systems. The unification of the theoretical and experimental work is the development or discovery of effective amino acid interactions that implicitly include the effects of aqueous solvent. We show that consideration of the full range of complexity of aqueous hydration forces such as many-body effects, long-ranged character of aqueous solvation, and the assumptions made about the degree of protein hydrophobicity can directly impact the observed structure, folding, and stability of model protein systems.
UR - http://www.scopus.com/inward/record.url?scp=20544474772&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=20544474772&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:20544474772
VL - 103
SP - 5424
EP - 5426
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
IS - 26
ER -