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PPTX
PPTX

... • Do we know all participants of the complex? • Do we have (open) sets of participants? • How do we indicate the depth of data available, i.e. compare Reactome import vs. manual curation? ...
Protein Degradation, Volume 1 ch01_p 1..9
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Coarse-grained normal mode analysis in structural biology
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Insulin-like Growth Factor-I (IGF-I) (Human) Cat. No. HEGFP
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Module 17 / Microscopic Level—The Sarcomere
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Publication JournalArticle (Originalarbeit in einer wissenschaftlichen
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Jake Wang - Critical Review of the Rosetta Algorithm
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HHMI meeting, FOLDING
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Screening for novel snake venom toxins using protein chemistry and molecular biology.
Screening for novel snake venom toxins using protein chemistry and molecular biology.

... We have been involved in isolation and characterization of novel toxins from snake venoms and identified a number of new toxins that belong to known family of toxins, but with different biological properties. We have also identified a few new families of snake venom toxins. The new toxins include (a ...
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Intrinsically disordered proteins



An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the last decades by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules.
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