scholarly journals Individuality of Amino Acid Residues in Protected Peptides. Conformational and β-Sheet Structure-Disrupted Behaviors of Resin-Bound Peptides

1989 ◽  
Vol 62 (3) ◽  
pp. 773-779 ◽  
Author(s):  
Mitsuaki Narita ◽  
Shizuko Isokawa ◽  
Shinya Honda ◽  
Hiroshi Umeyama ◽  
Hideaki Kakei ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Sheet Structure ◽  
Β Sheet ◽  
Protected Peptides

scholarly journals Peptide–dendron hybrids that adopt sequence-encoded β-sheet conformations

2018 ◽  
Vol 9 (40) ◽  
pp. 4994-5001
Author(s):  
Deborah A. Barkley ◽  
Sang Uk Han ◽  
Tadanori Koga ◽  
Jonathan G. Rudick
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Sheet Structure ◽  
Β Sheet

Patterning of the amino acid residues to which dendrons are grafted encodes a β-sheet structure in peptide–dendron hybrids.

An electronically enhanced chiral sum frequency generation vibrational spectroscopy study of lipid-bound cytochrome c

2015 ◽  
Vol 51 (1) ◽  
pp. 195-197 ◽  
Author(s):  
Khoi Tan Nguyen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Vibrational Spectroscopy ◽  
Amino Acid Residues ◽  
Spectroscopy Study ◽  
Sum Frequency ◽  
Anionic Phospholipids ◽  
Sheet Structure ◽  
Β Sheet

Electronically enhanced chiral SFG spectroscopy was employed to study the lipid bound cyt c in situ. It was directly observed that upon interacting with anionic phospholipids, the amino acid residues around the heme adopted the β-sheet conformation. In addition, the orientation of this newly formed β-sheet structure was found to be sensitive to the bulk pH.

scholarly journals Analysis of the Secondary Structure of β-Amyloid (Aβ42) Fibrils by Systematic Proline Replacement

2004 ◽  
Vol 279 (50) ◽  
pp. 52781-52788 ◽  
Author(s):  
Akira Morimoto ◽  
Kazuhiro Irie ◽  
Kazuma Murakami ◽  
Yuichi Masuda ◽  
Hajime Ohigashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amyloid Fibrils ◽  
Amino Acid Residues ◽  
Wild Type ◽  
Aβ Peptides ◽  
Amyloid Peptides ◽  
Aggregation Inhibitors ◽  
Β Amyloid ◽  
Β Sheet

Amyloid fibrils in Alzheimer's disease mainly consist of 40- and 42-mer β-amyloid peptides (Aβ40 and Aβ42) that exhibit aggregative ability and neurotoxicity. Although the aggregates of Aβ peptides are rich in intermolecular β-sheet, the precise secondary structure of Aβ in the aggregates remains unclear. To identify the amino acid residues involved in the β-sheet formation, 34 proline-substituted mutants of Aβ42 were synthesized and their aggregative ability and neurotoxicity on PC12 cells were examined. Prolines are rarely present in β-sheet, whereas they are easily accommodated in β-turn as a Pro-Xcorner. Among the mutants at positions 15-32, only E22P-Aβ42 extensively aggregated with stronger neurotoxicity than wild-type Aβ42, suggesting that the residues at positions 15-21 and 24-32 are involved in the β-sheet and that the turn at positions 22 and 23 plays a crucial role in the aggregation and neurotoxicity of Aβ42. The C-terminal proline mutants (A42P-, I41P-, and V40P-Aβ42) hardly aggregated with extremely weak cytotoxicity, whereas the C-terminal threonine mutants (A42T- and I41T-Aβ42) aggregated potently with significant cytotoxicity. These results indicate that the hydrophobicity of the C-terminal two residues of Aβ42 is not related to its aggregative ability and neurotoxicity, rather the C-terminal three residues adopt the β-sheet. These results demonstrate well the large difference in aggregative ability and neurotoxicity between Aβ42 and Aβ40. In contrast, the proline mutants at the N-terminal 13 residues showed potent aggregative ability and neurotoxicity similar to those of wild-type Aβ42. The identification of the β-sheet region of Aβ42 is a basis for designing new aggregation inhibitors of Aβ peptides.

scholarly journals Mutagenesis of Critical Amino Acid Residues in α-Helix and β-Sheet Structures of Brazzein

2011 ◽  
Vol 32 (11) ◽  
pp. 4106-4108 ◽  
Author(s):  
Hyun-Dong Do ◽  
Hyun-Joo Jo ◽  
Dong-Hyeon Jo ◽  
Kwang-Hoon Kong
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Critical Amino Acid ◽  
Α Helix ◽  
Β Sheet

Cloning and Characterization of Three Genes Encoding LMW-GSs from Triticum aestivum, Cultival Cheyenne

2012 ◽  
Vol 554-556 ◽  
pp. 1116-1120 ◽  
Author(s):  
Mei Rong Chen ◽  
Xing Shen ◽  
Lin Li ◽  
Song Qing Hu
Keyword(s):  
Amino Acid ◽  
Structure Prediction ◽  
Secondary Structure Prediction ◽  
Amino Acid Residues ◽  
Repetitive Domain ◽  
Genebank Accession ◽  
Genes Encoding ◽  
Α Helix ◽  
Β Sheet

Three low molecular weight subunit genes, named LMW-CND1 (GeneBank accession JQ780048), LMW-CND2 (GeneBank accession JQ779840), LMW-CND3 (GeneBank accession JQ779841), with a ORF of 1053 bp, 903 bp, 969 bp, respectively, were isolated from cv. Cheyenne and characterized detailed in molecular level. The proteins encoded by the genes, with 350, 300, 322 amino acid residues respectively, differ only in repetitive domain of sequences due to insertion or deletion of repeats in this domain. Highly similarity in amino-acid sequence between these three subunits and other published LMW-GSs was also observed, showing that all three genes published here are typical LMW-GS genes and closely related to the genes on chromosome 1D. Besides, secondary structure prediction of proteins indicated that, in the three LMW-GSs, random loop accounts for no less than 70 %, α-helix amounts to 26 %, average, and only 1.4 %~1.7 % is β-sheet.

Synthesis of a Hybrid Peptide with Both α- and β-Amino Acid Residues: Toward a New β-Sheet Nucleator

Tetrahedron ◽  
2000 ◽  
Vol 56 (50) ◽  
pp. 9739-9746 ◽  
Author(s):  
Benjamin W. Gung ◽  
Dong Zou ◽  
Yuko Miyahara
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Hybrid Peptide ◽  
Β Sheet

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.

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