【摘 要】
：
Our view on protein structure has changed dramatically due to the results of the genomic projects.The outcome of the genome projects first surprised us by t
【机 构】
：
InstituteofEnzymologyBiologicalResearchCenterHungarianAcademyofSciencesHungary
【出 处】
：
2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
Our view on protein structure has changed dramatically due to the results of the genomic projects.The outcome of the genome projects first surprised us by the fact that the number of proteins that can not fold up in aqueous solution but contains one or more transmembrane segments exceeds a quarter of the number of proteins coded in the genomes studied.Later we learned that even many of the "water soluble" proteins can not fold up without appropriate template macromolecules,like nucleic acids or certain proteins.What is more,some do not fold up at all and perform their function in an unstructured state.Some contains comparable sized structured and unstructured parts and there are many other non-conventional proteins too.In my talk I will present some of our recent results on predicting the topology of transmembrane proteins from amino acid sequences as well as extracting vital structural information on transmembrane proteins from various direct and indirect measurements.I will also present our method for predicting uns tinctured/disordered proteins and protein segments from amino acid sequences and our works on the characterization of the intermolecular interactions of these proteins.I will conclude some principles which can be extracted from these results that might shape our view on the functionally relevant structural forms of proteins.
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