Observation of a sterically unfavorable side-chain conformation in a leucyl residue: Crystal and molecular structure ofL-leucyl-L-leucine

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

Published:1994-09 Issue:9 Volume:34 Page:1139-1143
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Mitra Shome Nath,Subramanian E.

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference16 articles.

1. Specific recognition in the tertiary structure of β-sheets of proteins

2. Residue contacts in protein structures and implications for protein folding

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1. Self‐assembly of heterochiral, aliphatic dipeptides with Leu;Journal of Peptide Science;2023-12-18

2. High-pressure studies on l,l-dileucine crystals by Raman spectroscopy and synchrotron X-ray diffraction combined with DFT calculations;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2020-03

3. Tubular to spherical mesoscopic self‐assembly of C‐ and N‐termini capped dileucines;Peptide Science;2019-09-30

4. The Impact of Trifluoroacetic Acid on Peptide Cocrystallization: Multicomponent Crystals of l-Leu-l-Leu Dipeptides;Crystal Growth & Design;2018-06-22

5. Hydrophobic dipeptides: the final piece in the puzzle;Acta Crystallographica Section B Structural Science, Crystal Engineering and Materials;2018-05-24

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