Parallel Versus Antiparallel β‐Sheet Structure in Cyclic Peptide Hybrids Containing γ‐ or δ‐Cyclic Amino Acids

2020 ◽  
Vol 26 (26) ◽  
pp. 5846-5858 ◽  
Author(s):  
Martín Calvelo ◽  
Alejandro Lamas ◽  
Arcadio Guerra ◽  
Manuel Amorín ◽  
Rebeca Garcia‐Fandino ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cyclic Peptide ◽  
Sheet Structure ◽  
Β Sheet ◽  
Cyclic Amino Acids

scholarly journals Hybrid approach to analysis of β-sheet structures based on signal processing and statistical consideration

2010 ◽  
Vol 467 (2128) ◽  
pp. 1052-1072
Author(s):  
V. Vojisavljevic ◽  
E. Pirogova ◽  
D. M. Davidovic ◽  
I. Cosic
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Design ◽  
Hybrid Approach ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Spectra Analysis ◽  
Sheet Structure ◽  
The Relationship ◽  
Β Sheet

A number of biotechnology applications are based on protein design. For this design, the relationship between a protein’s primary structure and its conformation is of vital importance. A β-sheet is a common feature of a protein’s two-dimensional structure; therefore, elucidating the principles governing β-sheet structure and its stability is critical for understanding the protein-folding process. In the three-dimensional representation of protein molecules, C α carbon coordinates (carbon atom immediately adjacent to the carboxylate group) have often been employed instead of the complete set of coordinates for the corresponding residues. Using the C α carbon coordinates, we showed that particular amino acids are not randomly distributed within a β-sheet structure. On the basis of a new statistical approach for the analysis of a spatial distribution of amino acids in a protein, presented by their physico-chemical parameters, the electron–ion interaction potential (EIIP) and hydrophobicity, are described here. The relationship between amino acid positions inside the β-sheet and the EIIP and hydrophobicity parameters was established. The correlation between amino acid propensities related to the β-sheet was examined using multiple cross-spectra analysis. We also applied the continuous wavelet transform for the analysis of selected β-sheet structures using the EIIP and hydrophobicity parameters. The findings provide new insight into conformational propensities of amino acids for the adaption of β-sheet structures.

Use of hydrolases for the synthesis of cyclic amino acids

Tetrahedron ◽  
2004 ◽  
Vol 60 (3) ◽  
pp. 717-728 ◽  
Author(s):  
Richard C Lloyd ◽  
Michael C Lloyd ◽  
Mark E.B Smith ◽  
Karen E Holt ◽  
Jonathan P Swift ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cyclic Amino Acids

On the roles of the alanine and serine in the β-sheet structure of fibroin

2015 ◽  
Vol 197 ◽  
pp. 10-17 ◽  
Author(s):  
Juan Francisco Carrascoza Mayen ◽  
Alexandru Lupan ◽  
Ciprian Cosar ◽  
Attila-Zsolt Kun ◽  
Radu Silaghi-Dumitrescu
Keyword(s):  
Sheet Structure ◽  
Β Sheet

ChemInform Abstract: Oxidative Decarboxylation of Cyclic Amino Acids and Dehydrogenation of Cyclic Secondary Amines with Iodosobenzene.

ChemInform ◽  
1989 ◽  
Vol 20 (26) ◽  
Author(s):  
M. OCHIAI ◽  
M. INENAGA ◽  
Y. NAGAO ◽  
R. M. MORIARTY ◽  
R. K. VAID ◽  
...  
Keyword(s):  
Amino Acids ◽  
Secondary Amines ◽  
Oxidative Decarboxylation ◽  
Cyclic Amino Acids

H2O2-oxidation of α-aminoisobutyric and cyclic amino acids catalyzed by iron(III) isoindoline complexes

Polyhedron ◽  
2015 ◽  
Vol 89 ◽  
pp. 91-95 ◽  
Author(s):  
Dóra Lakk-Bogáth ◽  
Miklós Harasztia ◽  
Róbert Csonka ◽  
Gábor Speier ◽  
József Kaizer
Keyword(s):  
Amino Acids ◽  
H2o2 Oxidation ◽  
Cyclic Amino Acids
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