Multisegmented Hybrid Polymer Based on Oligo-Amino Acids: Synthesis and Secondary Structure in Solution and in the Solid State

2019 ◽  
Vol 52 (12) ◽  
pp. 4534-4544 ◽  
Author(s):  
Jan Freudenberg ◽  
Wolfgang H. Binder
Keyword(s):  
Amino Acids ◽  
Solid State ◽  
Secondary Structure ◽  
Hybrid Polymer ◽  
Structure In Solution

Supramolecular secondary helical structures in solid-state N-protected amino acids

Nanoscale ◽  
2020 ◽  
Vol 12 (40) ◽  
pp. 20610-20620
Author(s):  
Zhaohui Zong ◽  
Aiyou Hao ◽  
Pengyao Xing
Keyword(s):  
Amino Acids ◽  
Solid State ◽  
Secondary Structure ◽  
Helical Structures

Helix is an important secondary structure in proteins and polypeptides, which, however, has rarely been recognized in amino acids or their simple derivatives.

scholarly journals Characterization of porcine osteonectin extracted from foetal calvariae

1988 ◽  
Vol 253 (1) ◽  
pp. 139-151 ◽  
Author(s):  
C Domenicucci ◽  
H A Goldberg ◽  
T Hofmann ◽  
D Isenman ◽  
S Wasi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Secondary Structure ◽  
Type I Collagen ◽  
Culture Shock ◽  
Gel Filtration ◽  
Alpha Helix ◽  
Type I ◽  
Homologous Proteins ◽  
Compact Structure ◽  
Significant Difference

Osteonectin, extracted from foetal porcine calvariae with 0.5 M-EDTA, was purified to homogeneity by using gel filtration and polyanion anion-exchange fast protein liquid chromatography under dissociative conditions without the need of reducing agents. The purified protein migrated with an Mr of 40,300 on SDS/polyacrylamide gels and was similar to bovine osteonectin in both amino acid composition and in its ability to bind to hydroxyapatite in the presence of 4 M-guanidinium hydrochloride (GdmCl). However, unlike the bovine protein, porcine osteonectin did not bind selectively to hydroxyapatite when EDTA tissue extracts were used. In addition, purified porcine osteonectin did not show any apparent affinity for either native or denatured type I collagen, but did bind to serum albumin. Primary sequence analysis revealed an N-terminal alanine residue, with approximately one-half of the subsequent 35 residues identified as small hydrophobic amino acids and one-quarter as acidic amino acids. The only significant difference between the N-terminal sequences of the bovine and porcine proteins was the deletion of the tripeptide Val-Ala-Glu in porcine osteonectin. In contrast with bovine osteonectin, far-u.v.c.d. of porcine osteonectin revealed considerable secondary structure, of which 27% was alpha-helix and 39% was beta-sheet. Cleavage of the molecule with CNBr under non-reducing conditions generated five fragments, of which two major fragments (Mr 27,900 and 12,400) stained blue with Stains All, a reagent that stains sialic-acid-rich proteins/phosphate-containing proteins and/or Ca2+-binding proteins blue while staining other proteins pink. The 12,400-Mr fragment bound 45Ca2+ selectively, indicating a Ca2+-binding site in this part of the molecule. The 27,900-Mr fragment did not bind Ca2+, and since biosynthetic studies with 32PO4(3-) did not show phosphorylation of porcine osteonectin, this fragment is likely to be highly acidic. The incomplete cleavage of the molecule with CNBr and the ability of the molecule to regain its secondary structure after exposure to 7 M-urea are features consistent with the molecule having a compact structure that is stabilized by numerous disulphide bridges. The chemical and binding properties of porcine osteonectin are closely similar to the recently described ‘culture shock’, SPARC and BM-40 proteins, indicating that these are homologous proteins.

scholarly journals Synthesis of new Cα-tetrasubstituted α-amino acids

2009 ◽  
Vol 5 ◽  
Author(s):  
Andreas A Grauer ◽  
Burkhard König
Keyword(s):  
Amino Acids ◽  
Secondary Structure ◽  
Aromatic Aldehydes ◽  
Building Blocks ◽  
Reaction Conditions ◽  
Peptide Backbone ◽  
Aliphatic Aldehydes ◽  
New Class ◽  
Cyclic Amino Acids

Cα-Tetrasubstituted α-amino acids are important building blocks for the synthesis of peptidemimetics with stabilized secondary structure, because of their ability to rigidify the peptide backbone. Recently our group reported a new class of cyclic Cα-tetrasubstituted tetrahydrofuran α-amino acids prepared from methionine and aromatic aldehydes. We now report the extension of this methodology to aliphatic aldehydes. Although such aldehydes are prone to give aldol products under the reaction conditions used, we were able to obtain the target cyclic amino acids in low to moderate yields and in some cases with good diastereoselectivity.

scholarly journals Far infrared spectra of solid state aliphatic amino acids in different protonation states

2010 ◽  
Vol 132 (11) ◽  
pp. 115105 ◽  
Author(s):  
Aurélien Trivella ◽  
Thomas Gaillard ◽  
Roland H. Stote ◽  
Petra Hellwig
Keyword(s):  
Amino Acids ◽  
Solid State ◽  
Infrared Spectra ◽  
Far Infrared ◽  
Far Infrared Spectra

scholarly journals Production of single cell protein (SCP) and essentials amino acids from Candida utilis FMJ12 by solid state fermentation using mango waste supplemented with nitrogen sources

2018 ◽  
Vol 17 (23) ◽  
pp. 716-723 ◽  
Author(s):  
Kounbesioune SOMDA Marius ◽  
NIKIEMA Mahamadi ◽  
KEITA Ibrahim ◽  
MOGMENGA Iliassou ◽  
H. S. KOUHOUNDE Sonagnon ◽  
...  
Keyword(s):  
Amino Acids ◽  
Solid State ◽  
Single Cell ◽  
Solid State Fermentation ◽  
Candida Utilis ◽  
Nitrogen Sources ◽  
Single Cell Protein ◽  
Cell Protein
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