𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Study of the conformational profile of selected unnatural amino acid residues derived from l-phenylalanine

✍ Scribed by Jesus Gomez-Catalan; Juan J. Perez; Ana I. Jimenez; Carlos Cativiela

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
359 KB
Volume
5
Category
Article
ISSN
1075-2617

No coin nor oath required. For personal study only.

✦ Synopsis

The present work reports the results of a conformational study performed on seven unnatural amino acid residues and on its natural precursor, investigated by means of computational methods at the molecular mechanics level. Amino acid residues selected for the present study are derivatives of L-phenylalanine substituted at the h and/or i carbons. This series is composed of different linear analogs, including h-methyl, i-methyl and i-phenyl substituted with different stereochemistry. Analysis of the Ramachandran maps of the corresponding dipeptides in vacuo reveals their conformational preferences, to be used as guidance for the synthesis of constrained peptide analogs with desired conformational propensities. The available conformational space for every dipeptide is also analysed.

📜 SIMILAR VOLUMES

Conformation of peptides constructed fro
Conformation of peptides constructed from achiral amino acid residues Aib and ΔZPhe: Computational study of the effect of L/D- Leu at terminal positions
✍ Fateh Singh Nandel; Baldeep Khare 📂 Article 📅 2004 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 196 KB

## Abstract Conformational studies of the peptides constructed from achiral amino acid residues Aib and Δ^Z^Phe (I) Ac‐Aib‐Δ^Z^Phe‐NHMe (II), and Ac‐(Aib‐Δ^Z^Phe)~3~‐NHMe; peptides III–VI having L‐Leu or D‐Leu at either the N‐ or the C‐terminal position and of peptides VII–X having Leu residues in

Influence of D and L amino-acid residues
Influence of D and L amino-acid residues on the conformation of peptides in solution: A carbon-13 nuclear magnetic resonance study of cyclo(prolyl-leucyl)
✍ Roxanne Deslauriers; Z. Grzonka; Roderich Walter 📂 Article 📅 1976 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 375 KB 👁 1 views

## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp

The role of the Val57 amino-acid residue
The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants
✍ Sylwia Rodziewicz-Motowidło; Justyna Iwaszkiewicz; Renata Sosnowska; Paulina Cza 📂 Article 📅 2009 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 368 KB

## Abstract Human cystatin C (HCC) is one of the amyloidogenic proteins to be shown to oligomerize via a three‐dimensional domain swapping mechanism. This process precedes the formation of a stable dimer and proceeds particularly easily in the case of the L68Q mutant. According to the proposed mech