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Predicting conformational entropy of bond vectors in proteins by networks of coupled rotators
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10.1063/1.2969809
/content/aip/journal/jcp/129/9/10.1063/1.2969809
http://aip.metastore.ingenta.com/content/aip/journal/jcp/129/9/10.1063/1.2969809
View: Figures

Figures

Image of FIG. 1.
FIG. 1.

Top: Plot of the conformational entropy vs color coded as a function of the anisotropy of the effective potential (see text for the definition of ). Bottom: “Directional” entropies and of amide NH bond vectors.

Image of FIG. 2.
FIG. 2.

Plot of the predicted order parameters (top) and conformational entropy (bottom) in the protein calbindin. Values for the apo- and holo-calbindin are depicted by filled circles and open squares. The calcium-binding sites (residues 14–27 and 54–65) are indicated by shaded boxes.

Image of FIG. 3.
FIG. 3.

Differences of and between apo- and holo-calbindin. Only differences larger than the error bars are plotted. The red circles indicate NH vectors for which and (residues 5, 10, 12, 20, 21, 26, 27, 37, and 59).

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/content/aip/journal/jcp/129/9/10.1063/1.2969809
2008-09-05
2014-04-17
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Predicting conformational entropy of bond vectors in proteins by networks of coupled rotators
http://aip.metastore.ingenta.com/content/aip/journal/jcp/129/9/10.1063/1.2969809
10.1063/1.2969809
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