CONFORMATION AND MOLECULAR-DYNAMICS CALCULATIONS ON UTEROGLOBIN FRAGMENT-18-47
| Autor: | Stefano Mammi, Evaristo Peggion, Annalisa Pastore, Sabina Improta |
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| Přispěvatelé: | Improta, S, Pastore, A, Mammi, S, Peggion, E |
| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Protein Conformation Molecular Sequence Data Biophysics Sequence (biology) Biochemistry Micelle Protein Structure Secondary Biomaterials Molecular dynamics Animals Uteroglobin Amino Acid Sequence Protein secondary structure Mathematical Computing biology Fragment (computer graphics) Chemistry Organic Chemistry General Medicine Nuclear magnetic resonance spectroscopy Peptide Fragments Solutions Helix biology.protein Thermodynamics Rabbits |
| Popis: | The conformational properties of fragment 18–47 of rabbit uteroglobin in aqueous solution containing SDS micelles were investigated by two-dimensional nmr spectroscopy and molecular dynamics calculations. The fragment comprises helices II and III and the β-turn connecting the two helices. The nmr results and nmr-restrained molecular dynamics calculations showed that in the isolated fragment the elements of secondary structure present in the intact protein are preserved only in part. Specifically, a well-defined α-helix was found in the sequence 33–44, corresponding to helix III of uteroglobin, while the regions of helix II and β-turn are characterized by high flexibility in the fragment. © 1994 John Wiley & Sons, Inc. |
| Databáze: | OpenAIRE |
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