Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein
| Autor: | Zelda R. Wasserman, William F. DeGrado, Lynne Regan, Arlene Rockwell |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Denaturation Circular dichroism Flexibility (anatomy) Protein Conformation Molecular Sequence Data Protein design macromolecular substances Protein Engineering Biochemistry Protein Structure Secondary Motion Protein structure medicine Computer Simulation Amino Acid Sequence Molecular Biology Peptide sequence Helix bundle Chemistry Circular Dichroism Helix-Loop-Helix Motifs technology industry and agriculture Protein engineering Crystallography medicine.anatomical_structure Bundle Chromatography Gel Biophysics Cystine Peptides Oxidation-Reduction Research Article |
| Zdroj: | Protein Science. 3:2419-2427 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.5560031225 |
| Popis: | The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility. |
| Databáze: | OpenAIRE |
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