pH dependent conformation of physalaemin
| Autor: | K.G.R. Pachler, G. Hölzemann |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Magnetic Resonance Spectroscopy Protein Conformation Chemistry Physalaemin Stereochemistry Hydrogen bond Chemical shift Molecular Sequence Data Peptide Nuclear magnetic resonance spectroscopy Hydrogen-Ion Concentration Biochemistry Amino acid Turn (biochemistry) chemistry.chemical_compound Tachykinins Amino Acid Sequence Asparagine |
| Zdroj: | International Journal of Peptide and Protein Research. 34:139-147 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1989.tb01503.x |
| Popis: | The undecapeptide physalaemin was investigated by n.m.r. spectroscopy in DMSO solution under acidic and neutral conditions. Large changes of the NH chemical shifts and the temperature gradients of the NH protons occurred on going from pH 3.5 to pH 7.0 for residues around the charged amino acids Asp and Lys. At pH 3.5 the data are in accord with a flexible conformation of the peptide. The results at neutral pH are interpreted in terms of a folded structure having two interresidue and one intraresidue hydrogen bond. They include a beta turn with proline in position i + 1 and asparagine in position i + 2. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|