Beschreibung
- The analysis of membrane proteins is essential in genomic and proteomic-wide investigations. It is necessary and helpful to understand their structures and hence, mechanisms and regulation at the molecular level. Genome-wide investigations of membrane proteins have revealed a large number of short, distinct sequence motifs. These motifs support the understanding of the features that are important for establishing stability and functionality of the folded membrane protein in the membrane environment. Thus, membrane protein sequence motif analysis can be helpful in a number of applications, i.e. the investigation of mutant proteins and potential effects of mutagens. It is apparent that a specific three-dimensional protein structure depends on the information stored in the corresponding amino acid sequence. Thus, many in-silico approaches have been utilized extensively to make crucial advances in understanding membrane protein structures and functions. In this work, different meaningful statistical information obtained from sequence motif analyses have led to a novel understanding, how motifs interact spatially and thus contribute to build and stabilize membrane protein structures. Further, they play an important role in the classification of high-dimensional protein data. Our approach lacks of visualization outputs to fully unravel the complex associations between structural and functional motifs. These motifs describe the features that stabilize the folded conformation of membrane proteins and hints for family-specific participation and evaluation. Finally, these features are shown in a novel socalled 2.5 dimensional representation.