Peptide Models of Membrane Protein Folding
| Autor: | Charles M. Deber, Arianna Rath, David V. Tulumello |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Protein Folding biology Membrane transport protein Rational design Membrane Proteins Peptide Computational biology Biochemistry Transmembrane protein Folding (chemistry) Membrane protein chemistry biology.protein Peptides Peptide sequence Integral membrane protein |
| Zdroj: | Biochemistry. 48:3036-3045 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi900184j |
| Popis: | Given the central roles of membrane proteins in cellular processes ranging from nutrient uptake to cell-cell communication, as well as the importance of these proteins as drug targets, efforts to understand and control their structures are vital in human health and disease. The rational design of membrane proteins with modified properties is thus a highly desirable goal in molecular medicine and biotechnology. However, experimental data showing how individual transmembrane (TM) residues and/or segments direct the packing and folding of membrane proteins into biologically functional entities remain sparse. To address these questions in a systematic manner, helix-helix interactions between two (or more) TM segments must be identified and analyzed. Here we present an overview of the utilization of peptides as models of the TM segments of alpha-helical membrane proteins in uncovering the amino acid sequence motifs and interactions that build these molecules. TM peptide design and production strategies are discussed, and specific examples of the application of TM peptides to the study of membrane proteins are presented. We demonstrate that TM peptides can be routinely produced in sufficient quantities for biophysical analysis, are amenable to a variety of experimental techniques, and can effectively replicate the native helix-helix contacts and key aspects of the natural biological structures of membrane proteins. |
| Databáze: | OpenAIRE |
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