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| Carsten C. Mahrenholz*; Ingrid G. Abfalter*; Ulrich Bodenhofer; Rudolf Volkmer; Sepp Hochreiter. |
| *Overview* | Coiled coils are usually described as consisting of two up to seven α-helices that are wrapped around each other. They can associate as either homomeric or heteromeric structures and bind in parallel or antiparallel topologies. Another characteristic of all coiled coils is the periodic recurrence of a sequence [abcdefg]n called heptad repeat, where n denotes the heptad number. In these repeats, a and d are hydrophobic amino acids at core positions crucial for the tertiary structure. In contrast, the polar positions b, c, and f are hydrophilic and e and g are charged residues.
Due to their ability to oligomerize, coiled coils are involved in a variety of important cellular functions, either on their own or as part of... |
| Tipo: Poster |
Palavras-chave: Chemistry; Bioinformatics. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/4677/version/1 |
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| Carsten C. Mahrenholz; Victor Tapia; Rolf Stigler; Rudolf Volkmer. |
| There are several methods commonly used to measure protein-protein interactions and binding affinities. Quite contrary to most of these methods, protein- and peptide arrays on cellulose membranes or glass slides are suitable for high-throughput measurement, as they provide a higher density of probes and a multitude of peptide-protein interactions can be measured in parallel [1]. The most important application of the SPOT synthesis technique is to simultaneously detect a high number of peptides that have a strong binding affinity to defined targets. The validity of the results, however, depends on the ability of the detection system to indicate binding events whilst not interfering with the experiment itself through cross reaction. We tested three common... |
| Tipo: Poster |
Palavras-chave: Biotechnology; Chemistry. |
| Ano: 2010 |
URL: http://precedings.nature.com/documents/4448/version/1 |
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