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Seminars: Molecular and cellular biophysics WS04/05
Seminars: Molecular and cellular biophysics WS04/05

... cellular signaling and belong to the major target proteins of presently used medicaments. Inspite of their importance for most of the membrane proteins detailed moleczular structures and functions are missing. This section concerns structural principles of membrane protein folding and structure, as ...
sc-PDB: an annotated database of druggable binding sites from the
sc-PDB: an annotated database of druggable binding sites from the

... [1] Kellenberger, E., Muller, P., Schalon, C., Bret, G., Foata, N. and Rognan, D. (2006). sc-PDB: an Annotated Database of Druggable Binding Sites from the Protein Data Bank J. chem. Inf. Model. 46, 717-727. [2] Surgand, J.-S.; Rodrigo, J.; Kellenberger, E. and Rognan, D. (2006). A chemogenomic anal ...
The Structure of Cell Membranes - Biochemical Society Transactions
The Structure of Cell Membranes - Biochemical Society Transactions

... inner and mitochondria1 inner membranes. This is not true of bacterial outer membranes, which are probably not real membranes anyway. These former membranes can also serve a different purpose; they can be used to concentrate (hydrophobic) enzymes. This has a special advantage if these enzymes are mo ...
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Amino Acids as Protein Building Blocks

... Amino acids are most logically grouped according to the physical properties of their side chains. ...
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Additional file 1, Table S1. Summary of yeast two

... Additional file 3, Figure S1. Alignment of mouse (Mm) Hes1, Hes5 and Hes6 with Hes6-like proteins from zebrafish (Dr) (Her8a, Her8.2, Her13 and Hes6) and other species (Fr: Fugu rubripes, Ol: Oryzias latipes, Gg: Gallus gallus, Hs: Homo sapiens, Xt: Xenopus tropicalis). Protein domains are color-cod ...
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1 Corporation obtaining approval, the name of its representative

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PowerPoint 0.8MB - The Biomolecular Modeling & Computational

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... globular structure formed by bending and twisting of the polypeptide chain.  This process often means that the linear sequence of amino acids is folded into a compact globular structure.  The folding of the polypeptide chain is stabilized by multiple weak ,non covalent interactions .These interact ...
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Spectrophotometric methods for determination of proteins

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Table S4: Domains present in a network region characterized by

... Members of this family are found in plants, lower eukaryotes, and bacteria and the chloroplast where it is annotated as Ycf49 or Ycf49-like. The function is not known though several members are annotated as putative membrane proteins. This family is conserved in Cyanobacteria. Several members are an ...
MCB Seminar 4B, 2015 : Translation
MCB Seminar 4B, 2015 : Translation

... unable to fuse to the cis Golgi. In addition, after some time the formation of COPII vesicles also stops. Explain these observations. 15. A mammalian cell has a mutation in Ire1a protein that drastically increases its affinity to a BiP chaperon. The cell however responds almost normally to elevated ...
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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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