Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics
With the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13C, 15N and ¹H chemical shift dispersion to predict the amount of secondary structure of unassigned proteins from their 15N- and/or 13C-edit...
Main Authors: | Vitor Hugo Moreau, Ana Paula Valente, Fábio C.L. Almeida |
---|---|
Format: | Article |
Language: | English |
Published: |
Sociedade Brasileira de Genética
2006-01-01
|
Series: | Genetics and Molecular Biology |
Subjects: | |
Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030 |
Similar Items
-
Structural Proteomics of Herpesviruses
by: Baptiste Leroy, et al.
Published: (2016-02-01) -
Zero in on Key Open Problems in Automated NMR Protein Structure Determination
by: Abbas, Ahmed
Published: (2015) -
Structure of prion β-oligomers as determined by structural proteomics
by: Serpa, Jason John
Published: (2017) -
Protein Structure Validation and Identification from Unassigned Residual Dipolar Coupling Data Using 2D-PDPA
by: Homayoun Valafar, et al.
Published: (2013-08-01) -
The Structural Shifts and Transformations as Processes and Results of Structural Changes in the Economy
by: Pelekh Oksana B.
Published: (2018-03-01)