Synthesis and Hydrogen Bonding Capabilities of Biphenyl-Based Amino Acids Designed To Nucleate β-Sheet Structure

1996 ◽  
Vol 61 (9) ◽  
pp. 3127-3137 ◽  
Author(s):  
Carey L. Nesloney ◽  
Jeffery W. Kelly
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonding ◽  
Sheet Structure ◽  
Β Sheet

Amyloid structure

2014 ◽  
Vol 56 ◽  
pp. 1-10 ◽  
Author(s):  
Louise Serpell
Keyword(s):  
Hydrogen Bonding ◽  
Sequence Homology ◽  
Amyloid Fibrils ◽  
Side Chains ◽  
Primary Sequence ◽  
Sheet Structure ◽  
Β Sheets ◽  
The Stability ◽  
Β Sheet ◽  
Proteins And Peptides

Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures, lending further strength and stability to the resulting fibres. The fact that so many proteins and peptides form amyloid structures under suitable conditions, seems to suggest that the sequence of the precursor is unimportant. However, it is now clear that side chains play a central role in forming interactions between several β-sheets to further stabilize and regulate the structures. The primary sequence plays a central role in determining the rate of fibril formation, the stability of the resulting structure to degradation and the final morphology of the fibrils. The side chains regulate the elongation and growth, and also the lateral association of the protofilament and fibrils, having a significant impact on the final architecture.

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

POLYMERIZATION OF DIACETYLENE USING β-SHEET AS A TEMPLATE

2006 ◽  
Vol 20 (25n27) ◽  
pp. 3872-3877 ◽  
Author(s):  
TAKESHI MORI ◽  
YOICHI FUKAWA ◽  
KENJI SHIMOYAMA ◽  
KEIJI MINAGAWA ◽  
MASAMI TANAKA
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Degree Of Polymerization ◽  
The Other ◽  
Unit Distance ◽  
Amide Bonds ◽  
Cleavage Process ◽  
Sheet Structure ◽  
High Degree ◽  
Β Sheet

In the parallel and anti-parallel β-sheet structures, hydrogen bonding arises between the amide bonds of the peptide chains to arrange them with a distance of ca. 5 Å. That distance matched with the repeating unit distance of polydiacetylene. In this study, the effectiveness of the β-sheet as a template for the polymerization of diacetylene was examined by using diacetylene-introduced oligopeptides. The diacetylene-introduced amino acid (Thr(DA)) was synthesized from L-threonine. Though peptides Ac-Thr(DA)-NHMe and Ac -[ Thr(DA) ]2- NHMe formed anti-parallel β-sheet, they showed slight or no polymerization in both of the solid and the solution states. On the other hand, Ac -[ Thr(DA) ]5- NHMe and 11mer peptide with a Thr(DA) in the center of the sequence contained anti-parallel β-sheet structure and formed polydiacetylene of high degree of polymerization with high conversion during the cleavage process of the peptide from resin in the solution. This result indicated that the preorganization of the peptide through the β-sheet formation was necessary for the polymerization of diacetylene group. Thus, the β-sheet motif was effective template for the polymerization of diacetylene.

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.

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

scholarly journals Hydrogen bonding in melamine compounds of amino acids

2014 ◽  
Vol 70 (a1) ◽  
pp. C534-C534
Author(s):  
Nasreddine Ghouari ◽  
Nourreedine Benali-Cherif
Keyword(s):  
Amino Acids ◽  
Hydrogen Bonding ◽  
Nitric Acid ◽  
Organic Cation ◽  
X Ray Diffraction ◽  
X Ray ◽  
Hybrid Compounds ◽  
Amino Butyric Acid ◽  
3D Network ◽  
Bonding Electron

The theme of this work is part of the study of intermolecular interactions that hold the crystal structures of hybrid compounds based sulphuric acid, nitric acid, Melamine, Diethylamine, L-(+) - glutamic acid, DL-2-amino butyric acid. The aim of this work is to enlarge our laboratory researches [1-3] and methods in synthesis of new hybrid compounds consisting in organic cation(s) and mineral anion(s). We have obtained single crystals of a few samples after several trials and we plan to synthesize and characterize these crystals by X-ray diffraction, FTIR and Raman. The crystals structures allow us to study the 3D network hydrogen bonding, electron density and collect several other informations useful in FTIR and Raman studies of these hybrid compounds.

scholarly journals Probing the Role of Backbone Hydrogen Bonding in a Critical β Sheet of the Extracellular Domain of a Cys-Loop Receptor

ChemBioChem ◽  
2009 ◽  
Vol 10 (8) ◽  
pp. 1385-1391 ◽  
Author(s):  
Kristin R. Gleitsman ◽  
Henry A. Lester ◽  
Dennis A. Dougherty
Keyword(s):  
Hydrogen Bonding ◽  
Extracellular Domain ◽  
Β Sheet
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