✦ LIBER ✦

Conformations of peptides containing 1-aminocyclohexanecarboxylic acid (Acc6). Crystal structures of two model peptides

✍ Scribed by BARDI, R. ;PIAZZESI, A.M. ;TONIOLO, C. ;SUKUMAR, M. ;RAJ, P. ANTONY ;BALARAM, P.

Book ID: 115098346
Publisher: Wiley (Blackwell Publishing)
Year: 2009
Tongue: English
Weight: 633 KB
Volume: 25
Category: Article
ISSN: 0367-8377
DOI: 10.1111/j.1399-3011.1985.tb02220.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Stereochemistry of peptides containing 1

Stereochemistry of peptides containing 1-aminocyclopentanecarboxylic acid (Acc5): Solution and solid-state conformations of Boc-Acc5-Acc5-NHMe

✍ R. Bardi; A. M. Piazzesi; C. Toniolo; M. Sukumar; P. Balaram 📂 Article 📅 1986 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 507 KB

The conformational analysis of a protected homodipeptide of 1-aminocyclopentanecarboxylic acid (Acc5) has been carried out. 'H-nmr studies establish a p-turn conformation for Boc-Acc'. Acc'-NHMe in chloroform and dimethylsulfoxide solutions involving the methylamide NH in an intramolecular hydrogen

Experimental conformational study of two

Experimental conformational study of two peptides containing α-aminoisobutyric acid. Crystal structure of N-acetyl-α-aminoisobutyric acid methylamide

✍ A. Aubry; J. Protas; G. Boussard; M. Marraud; J. Neel 📂 Article 📅 1978 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 789 KB

Some theoretical studies have predicted that the conformational freedom of the cy-aminoisobutyric acid (H-Aib-OH) residue is restricted to the a-helical region of the Ramachandran map. In order to obtain conformational experimental data, two model peptide derivatives, MeCO-Aib-NHMe 1 and Bu'CO-LPro-

Conformations of β-amino acid residues i

Conformations of β-amino acid residues in peptides: X-ray diffraction studies of peptides containing the achiral residue 1-aminocyclohexaneacetic acid, β3,3Ac6c

✍ Prema G. Vasudev; Rajkishor Rai; Narayanaswamy Shamala; Padmanabhan Balaram 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 837 KB

## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides

Nonstandard Amino Acids in Conformationa

Nonstandard Amino Acids in Conformational Design of Peptides. Helical Structures in Crystals of 5-10 Residue Peptides Containing Dipropylglycine and Dibutylglycine

✍ Karle, Isabella L.; Balaji Rao, R.; Prasad, Sudhanand; Kaul, Ramesh; Balaram, P. 📂 Article 📅 1994 🏛 American Chemical Society 🌐 English ⚖ 749 KB

β-Turn conformations in crystal structur

β-Turn conformations in crystal structures of model peptides containing α,α-Di-n-propylglycine and α,α-Di-n-butylglycine

✍ M. Crisma; G. Valle; C. Toniolo; Sudhanand Prasad; R. Balaji Rao; P. Balaram 📂 Article 📅 1995 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 515 KB

Erratum: “Conformations of β-amino acid

Erratum: “Conformations of β-amino acid residues in peptides: X-ray diffraction studies of peptides containing the achiral residue 1-aminocyclohexaneacetic acid, β3,3Ac6c”

✍ Prema G. Vasudev; Rajkishor Rai; Narayanaswamy Shamala; Padmanabhan Balaram 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 44 KB 👁 1 views

The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.