2019
DOI: 10.1007/978-1-4939-9161-7_4
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Computational Prediction of Secondary and Supersecondary Structures from Protein Sequences

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Cited by 11 publications
(8 citation statements)
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“…Secondary structure predictors are usually classified in three classes or “generations,” according to their theoretical basis and procedures (see refs. and for extensive reviews). First‐generation methods analyze individual propensities of amino acids on an almost purely statistical basis, whereas second‐generation procedures take into account the neighboring residues and carry out the prediction in sliding segments (windows) of amino acids.…”
Section: Chameleon Sequencesmentioning
confidence: 99%
“…Secondary structure predictors are usually classified in three classes or “generations,” according to their theoretical basis and procedures (see refs. and for extensive reviews). First‐generation methods analyze individual propensities of amino acids on an almost purely statistical basis, whereas second‐generation procedures take into account the neighboring residues and carry out the prediction in sliding segments (windows) of amino acids.…”
Section: Chameleon Sequencesmentioning
confidence: 99%
“…The huge amount of protein sequences that lack the residue-level annotations has motivated the development of hundreds of computational methods that predict these annotations from the sequences. For instance, there are over 60 predictors of the secondary structure [5] , [6] , [7] , over 100 predictors of the intrinsic disorder [8] , [9] , [10] , [11] , [12] , and close to 40 predictors of the residues that bind nucleic acids [13] , [14] , [15] . Some of these methods are heavily used, which can be indirectly measured by their citations.…”
Section: Introductionmentioning
confidence: 99%
“…Availability of the many sequence-based predictors of the residue-level annotations has spurred numerous studies that survey and compare these tools [1] , [2] , [5] , [6] , [7] , [8] , [9] , [10] , [11] , [13] , [14] , [15] , [29] , [30] , [31] , [32] , [33] , [34] , [35] , [36] , [37] , [38] , [39] , [40] , [41] , [42] , [43] , [44] , [45] , [46] . A large portion of these studies focuses on the empirical comparative assessment of their predictive performance.…”
Section: Introductionmentioning
confidence: 99%
“…[15] In the natural world, information is encoded within the amino acid sequence of proteins to direct their folding and therefore function (Figure 1A). [16] Such structure-activity relationships inspired ab ottom-up construction of functional [17] and cavity-containing [18] proteins,w hich is at the forefront of biochemistry research. [19] On the other hand, supramolecular chemists have approached this problem by creating sequence-defined foldamers [20] and chiral cavitands [21] for studying molecular encapsulation.…”
Section: Introductionmentioning
confidence: 99%