- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2105
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
RDb2C2: an improved method to identify the residue-residue pairing in β strands ; volume:21 ; number:1 ; day:3 ; month:4 ; year:2020 ; pages:1-12 ; date:12.2020
BMC bioinformatics ; 21, Heft 1 (3.4.2020), 1-12, 12.2020
- Creator
-
Shao, Di
Mao, Wenzhi
Xing, Yaoguang
Gong, Haipeng
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1186/s12859-020-3476-z
- URN
-
urn:nbn:de:101:1-2020062121414660955736
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
2025-08-14T10:56:45+0200
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Shao, Di
- Mao, Wenzhi
- Xing, Yaoguang
- Gong, Haipeng
- SpringerLink (Online service)
Other Objects (12)
Identification of residue pairing in interacting β-strands from a predicted residue contact map
Protein binding hot spots and the residue-residue pairing preference: a water exclusion perspective
General formulation of the sector-improved residue subtraction
Bayesian statistical approach for protein residue-residue contact Prediction
ResidueFinder: extracting individual residue mentions from protein literature
A conformation ensemble approach to protein residue-residue contact
Waste residue composites
Predicting protein residue-residue contacts using random forests and deep networks
The residue of uniqueness
The residue of uniqueness
Four-dimensional formulation of the sector-improved residue subtraction scheme
RRCRank: a fusion method using rank strategy for residue-residue contact prediction
Identification of residue pairing in interacting β-strands from a predicted residue contact map
Protein binding hot spots and the residue-residue pairing preference: a water exclusion perspective
General formulation of the sector-improved residue subtraction
Bayesian statistical approach for protein residue-residue contact Prediction
ResidueFinder: extracting individual residue mentions from protein literature
A conformation ensemble approach to protein residue-residue contact
Waste residue composites
Predicting protein residue-residue contacts using random forests and deep networks
The residue of uniqueness
The residue of uniqueness
Four-dimensional formulation of the sector-improved residue subtraction scheme
RRCRank: a fusion method using rank strategy for residue-residue contact prediction
Identification of residue pairing in interacting β-strands from a predicted residue contact map
Protein binding hot spots and the residue-residue pairing preference: a water exclusion perspective
General formulation of the sector-improved residue subtraction
Bayesian statistical approach for protein residue-residue contact Prediction
ResidueFinder: extracting individual residue mentions from protein literature
A conformation ensemble approach to protein residue-residue contact
Waste residue composites
Predicting protein residue-residue contacts using random forests and deep networks
The residue of uniqueness
The residue of uniqueness
Four-dimensional formulation of the sector-improved residue subtraction scheme