The Estimation of the β-Sheet-Structure Stability of Protected Peptides in Organic Solvents
- 1 February 1993
- journal article
- Published by Oxford University Press (OUP) in Bulletin of the Chemical Society of Japan
- Vol. 66 (2), 489-493
- https://doi.org/10.1246/bcsj.66.489
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The Classification of Twenty Common Amino Acid Residues in Protected Peptides by Their β-Sheet-Structure-Stabilizing Potentials, SPβ, and Its Application to Peptide SynthesisBulletin of the Chemical Society of Japan, 1993
- Weak dependence of octapeptide solubility in organic solvents on the amino acid sequence*International Journal of Peptide and Protein Research, 1989
- The β-Sheet Structure-Disrupting Potential of Electron-Donor and -Acceptor Solvents and Role of Mixed Solvents in Solvation of PeptidesBulletin of the Chemical Society of Japan, 1989
- Synthesis and solubility properties of peptide fragments of human hemoglobin α‐chain (123‐136)International Journal of Peptide and Protein Research, 1988
- The structure and dynamics of ribosomal protein L12Biochimie, 1987
- Peptide synthesis by fragment condensation on a soluble polymer support. 8. Maximum peptide chain lengths of carboxyl component peptides for effective coupling reactions with amino component peptides anchored to soluble and cross-linked polystyrene supportsMacromolecules, 1987
- Structure of the C-terminal domain of the ribosomal protein from Escherichia coli at 1.7 ÅJournal of Molecular Biology, 1987
- Critical Peptide Size for Insolubility Caused by a β-Sheet Aggregation and Solubility Improvement in Hydrophobic Peptides by Replacement of Alanine Residues with α-Aminoisobutyric Acid ResiduesBulletin of the Chemical Society of Japan, 1985
- Liquid-phase peptide synthesis by fragment condensation on soluble polymer support. 7. Influence of polymer support cross-linking on the coupling reactions of large carboxyl-component peptides with polymer-bound amino-component peptidesMacromolecules, 1985
- The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in OligopeptidesBulletin of the Chemical Society of Japan, 1985