Author: Li, Chun; Zhao, Jialing; Wang, Changzhong; Yao, Yuhua
Title: Protein Sequence Comparison and DNA-binding Protein Identification with Generalized PseAAC and Graphical Representation Document date: 2018_2_23
ID: u1imic5l_1
Snippet: DNA-binding proteins (DNA-BPs) are very important functional proteins in a cell. These proteins play vital roles in various cellular processes, including DNA replication, transcription, regulation of gene expression, packaging, and other activities associated with DNA [1] [2] [3] [4] [5] . It is therefore substantially important to distinguish DNA-BPs from non-DNA-binding proteins (NBPs). In the past, many experimental and computational technique.....
Document: DNA-binding proteins (DNA-BPs) are very important functional proteins in a cell. These proteins play vital roles in various cellular processes, including DNA replication, transcription, regulation of gene expression, packaging, and other activities associated with DNA [1] [2] [3] [4] [5] . It is therefore substantially important to distinguish DNA-BPs from non-DNA-binding proteins (NBPs). In the past, many experimental and computational techniques have been developed for identifying DNA-BPs. Experimental techniques can provide a clear-cut answer to a query protein. However, the experimental methods are cost-intensive and time-consuming, and thus impractical for large datasets [3] [4] [5] [6] [7] . Computational methods can be broadly divided into two categories: structure-based method and sequence-based *Address correspondence to this author at the School of Mathematics and Statistics, Hainan Normal University, Haikou 571158, China; Tel: +86-898-65883210; E-mail: [email protected] method. The former can discriminate DNA-binding and nonbinding proteins with high accuracy, but these methods can't be employed in high throughput annotation, as they require the structure information of a query protein [1] . Though tremendous progress has been achieved in experimental determination of protein structures in the past five decades, it can't keep pace with the explosive growth of sequence information resulting from modern sequencing technology [8] . Yet as suggested by Anfinsen [9] , proteins contain within their amino acid sequences enough information to determine their native conformation. Therefore, it is more promising to use sequence-based methods to identify DNA-BPs.
Search related documents:
Co phrase search for related documents- protein structure and sequence base: 1, 2, 3
- protein structure and sequence information: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21
- protein structure and sequencing technology: 1
- protein structure and structure base: 1, 2, 3, 4, 5
- protein structure and structure information: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52
- protein structure and tremendous progress: 1
- protein structure experimental determination and structure information: 1
- protein vital role play and vital role: 1, 2, 3, 4, 5, 6
- protein vital role play and vital role play: 1, 2, 3, 4, 5, 6
- query protein and sequence information: 1, 2
- sequence base and structure base: 1, 2, 3, 4, 5, 6, 7, 8
- sequence base and structure information: 1, 2
- sequence information and structure base: 1, 2
- sequence information and structure information: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22
- sequence information and tremendous progress: 1
- sequencing technology and throughput annotation: 1
- sequencing technology and tremendous progress: 1
- sequencing technology and vital role: 1, 2, 3
- sequencing technology and vital role play: 1, 2
Co phrase search for related documents, hyperlinks ordered by date