✦ LIBER ✦

The fixed conformation of the leucyl side-chain in a tripeptide

✍ Scribed by Raymond J. Abraham; J. Timothy Jackson; W. Anthony Thomas

Publisher: John Wiley and Sons
Year: 1980
Tongue: English
Weight: 166 KB
Volume: 14
Category: Article
ISSN: 0749-1581
DOI: 10.1002/mrc.1270140625

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The complete analysis of the ^1^H NMR spectrum of the leucyl side‐chain of a tripeptide allows the deduction of the conformation of this side‐chain. In the peptide, in contrast to the free amino acid, the side‐chain is in a single fixed conformation.

📜 SIMILAR VOLUMES

Observation of a sterically unfavorable

Observation of a sterically unfavorable side-chain conformation in a leucyl residue: Crystal and molecular structure of L-leucyl–L-leucine · DMSO solvate

✍ Shome Nath Mitra; E. Subramanian 📂 Article 📅 1994 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 340 KB

Structure and conformation of the cortis

Structure and conformation of the cortisone side chain

✍ A. Cooper; W. L. Duax 📂 Article 📅 1969 🏛 John Wiley and Sons 🌐 English ⚖ 315 KB

Modeling of the Amino Acid Side Chain Ef

Modeling of the Amino Acid Side Chain Effects on Peptide Conformation

✍ Katrin Sak; Mati Karelson; Jaak Järv 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 76 KB

Semiempirical AM1 calculations were carried out for quantum-chemically optimized minimum energy conformations of peptides (Ala) 4 -X-(Ala) 4 , where X stands for different L-␣amino acids (Ala,

Molecular dynamics simulations of Trp si

Molecular dynamics simulations of Trp side-chain conformational flexibility in the gramicidin A channel

✍ Nathan C. Bingham; Natasha E. C. Smith; Timothy A. Cross; David D. Busath 📂 Article 📅 2003 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 338 KB 👁 2 views

Gramicidin A (gA) is prototypical peptide antibiotic and a model ion channel former. Configured in the solid-state NMR beta(6.5)-helix channel conformation, gA was subjected to 1-ns molecular dynamics (MD) gas phase simulations using the all-atom charmm22 force field to ascertain the conformational

ChemInform Abstract: A Stereospecific El

ChemInform Abstract: A Stereospecific Elimination to Form Dehydroamino Acids: Synthesis of the Phomopsin Tripeptide Side Chain.

✍ Michelle M. Stohlmeyer; Hiroko Tanaka; Thomas J. Wandless 📂 Article 📅 2010 🏛 John Wiley and Sons ⚖ 37 KB 👁 1 views

Critical assessment of side-chain confor

Critical assessment of side-chain conformational space sampling procedures designed for quantifying the effect of side-chain environment

✍ R. Gautier; P. Tufféry 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 148 KB

## Abstract We introduce a family of procedures designed to sample side‐chain conformational space at particular locations in protein structures. These procedures (CRSP) use intensive cycles of random assignment of side‐chain conformations followed by minimization to determine all the conformations