Modulation of the Peptide Backbone Conformation by the Selenoxo Photoswitch

2010 ◽  
Vol 132 (22) ◽  
pp. 7578-7579 ◽  
Author(s):  
Yun Huang ◽  
Günther Jahreis ◽  
Christian Lücke ◽  
Dirk Wildemann ◽  
Gunter Fischer
1991 ◽  
Vol 266 (28) ◽  
pp. 18460-18468
Author(s):  
A.R. Dentino ◽  
P.A. Raj ◽  
K.K. Bhandary ◽  
M.E. Wilson ◽  
M.J. Levine

Biochemistry ◽  
2012 ◽  
Vol 51 (27) ◽  
pp. 5463-5475 ◽  
Author(s):  
Knut Kölbel ◽  
Christian Ihling ◽  
Uwe Kühn ◽  
Ines Neundorf ◽  
Silke Otto ◽  
...  

2021 ◽  
Vol 77 (2) ◽  
pp. 249-266
Author(s):  
Dale E. Tronrud ◽  
P. Andrew Karplus

While broadening the applicability of (φ/ψ)-dependent target values for the bond angles in the peptide backbone, sequence/conformation categories with too few residues to analyze via previous methods were encountered. Here, a method of describing a conformation-dependent library (CDL) using two-dimensional Fourier coefficients is reported where the number of coefficients for individual categories is determined via complete cross-validation. Sample sizes are increased further by selective blending of categories with similar patterns of conformational dependence. An additional advantage of the Fourier-synthesis-based CDL is that it uses continuous functions and has no artifactual steps near the edges of populated regions of φ/ψ space. A set of libraries for the seven main-chain bond angles, along with the ω and ζ angles, was created based on a set of Fourier analyses of 48 368 residues selected from high-resolution models in the wwPDB. This new library encompasses both trans- and cis-peptide bonds and outperforms currently used discrete CDLs.


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