PRISMΔDB

Analyze how specific documents activate the features of the SAE. Select a dataset, a run and a document to begin.

Active Features

1543

0.0
Details List
#2808 Feature 2808
3.2
#1549 Feature 1549
2.8
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2.8
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2.7
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2.6
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2.5
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2.5
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2.5
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2.4
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2.4
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2.4
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2.3
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2.3
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2.2
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2.1
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2.1
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2.0
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2.0
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2.0
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2.0
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1.9
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1.9
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1.9
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1.9
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1.8
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1.7
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1.7
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1.7
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1.7
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1.7
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1.7
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1.6
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1.6
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1.6
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1.6
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1.6
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1.6
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1.6
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1.6
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1.6
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.5
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1.4
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1.4
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1.4
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1.4
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1.4
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1.4
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.3
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.2
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.1
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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1.0
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0.9
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Document Content

Peptides of aminoxy acids as foldamers.
This Feature Article summarizes our efforts in developing a new family of foldamers from alpha-, beta- and gamma-aminoxy acids. From a series of conformational studies, we demonstrate that peptides consisting of aminoxy acids adopt several well-defined secondary structures, such as alpha N-O turns (which feature an eight-membered-ring hydrogen bond), beta N-O turns (a nine-membered-ring hydrogen bond), gamma N-O turns (a ten-membered-ring hydrogen bond), 1.8(8) helices (consecutive homochiral alpha N-O turns), 7/8 helices (alternating alpha N-O turns and gamma-turns), 1.7(9) helices (consecutive beta N-O turns), reverse turns (consecutive heterochiral alpha N-O turns) and sheet-like structures.