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Monday, July 27, 2020 | History

4 edition of Structure, Self-organization and Stability of Proteins found in the catalog.

Structure, Self-organization and Stability of Proteins

experiments and models : Faltertage 2000 : Leopoldina Symposium : Leucorea in Wittenberg, Germany, September 21, 2000 to September 23, 2000

by Leopoldina Symposium on the Structure, Self-organization and Stability of Proteins (2000 Wittenberg, Germany)

  • 9 Want to read
  • 5 Currently reading

Published by Deutsche Akademie der Naturforscher Leopoldina in Halle .
Written in English

    Subjects:
  • Proteins -- Structure -- Congresses.,
  • Proteins -- Conformation -- Congresses.,
  • Protein folding -- Congresses.

  • Edition Notes

    Statementorganized by the Deutsche Akademie der Naturforscher Leopoldina and the Martin-Luther-Universität Halle-Wittenberg ; organizer, Rainer Jaenicke ; [redaktion, Michael Kaasch und Joachim Kaasch]
    GenreCongresses.
    SeriesNova acta Leopoldina., Nr. 16
    ContributionsJaenicke, R. 1930-, Kaasch, Michael., Kaasch, Joachim., Deutsche Akademie der Naturforscher Leopoldina., Martin-Luther-Universität Halle-Wittenberg.
    Classifications
    LC ClassificationsQP551 .L463 2000
    The Physical Object
    Pagination200 p. :
    Number of Pages200
    ID Numbers
    Open LibraryOL3636136M
    ISBN 103830451075
    LC Control Number2002438023
    OCLC/WorldCa49946510

      The book summarizes and presents in a systematic way the results of several decades of worldwide fundamental research on protein physics, structure and folding. It describes many simple physical models aimed to help a reader to estimate and predict of .   CMU proteins bind MTs and are associated with membranes. However, loss of CMU function was not sufficient to detach MTs from the plasma membrane and the authors hypothesized that CMUs may be part of a protein complex that links MTs to the plasma membrane (Liu et al., ). CC proteins directly bound MTs and promoted MT recovery after salt by:

    Programming the Internal Structure and Stability of Helical Pores Self-Assembled from Dendritic Dipeptides via the Protective Groups of the PeptideCited by: Abstract. Inspection of globular proteins shows that the most common protein structures are those that have some advantage in stability. This would cause no wonder if the advantages were not so small and the difference in occurrence was not so by:

    •The 3D structure of proteins has been shown already in by Hoppe-Zeiler. •Hemoglobin crystals: in a crystal each atom occupies a unique place. •The question whether the File Size: 2MB. This book describes a new family of bio-polymer gels made from cytoskeletal proteins - actin, microtubule, and tropomyosin. The importance of the gel state with multi-scale hierarchical structure is emphasized to utilize emergent functions in living organisms.


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Structure, Self-organization and Stability of Proteins by Leopoldina Symposium on the Structure, Self-organization and Stability of Proteins (2000 Wittenberg, Germany) Download PDF EPUB FB2

Structure, self-organization and stability of proteins: experiments and models ; Leopoldina symposium. Self-organization, also called (in the social sciences) spontaneous order, is a process where some form of overall order arises from local interactions between parts of an initially disordered process can be spontaneous when sufficient energy is available, not needing control by any external agent.

It is often triggered by seemingly random fluctuations, amplified by positive feedback. Protein Self-Organization: Lessons from the Min System Article (PDF Available) in Annual Review of Biophysics 40(1) June with Reads How we measure 'reads'.

Notice that the self-organization of 3D structures of proteins (and RNAs, and crystals) results from the Structure to thermodynamic stability, which distinguishes this self-organization from the more widely discussed self-organization of the “order from disorder” class (existing in oscillating Belousov-Zhabotinsky chemical reactions, in.

Self-organization in protein structures has been measured in a variety of Self-organization and Stability of Proteins book such as energy frustration [25], hydrophobic interactions [26], and folding index [27].

This self-organizing nature. Cold-shock proteins from B. subtilis, B. caldolyticus and T. maritima differ significantly in both their sequences and thermal stabilities (ΔG N→U = 11, 20 and 26 kJ/mol, respectively), but show similar, extremely fast folding kinetics (k U→N =, s −1).The lack of correlation between the thermodynamic stability and folding rate indicates that proteins with a more stable Cited by: The structure and function of cells are critically dependent on membranes, which not only separate the interior of the cell from its environment but also define the internal compartments of eukaryotic cells, including the nucleus and cytoplasmic organelles.

The formation of biological membranes is based on the properties of lipids, and all cell membranes share a common structural organization. Three types of cytoskeletal filaments are common to many eucaryotic cells and are fundamental to the spatial organization of these cells.

Intermediate filaments provide mechanical strength and resistance to shear stress. Microtubules determine the positions of membrane-enclosed organelles and direct intracellular transport.

Actin filaments determine the shape of the cell's surface and are Cited by: 2. Proteins are synthesized in the form of a flexible polypeptide chain that is capable of assuming a vast number of configurations; the transformation of this chain into a specific, relatively rigid three-dimensional structure is called folding--a remarkable process of self-organization.

Thermodynamic Theory of Structure, Stability and Fluctuations, Wiley-Interscience, London. ISBN ^ Bernard Feltz et al (). Self-organization and Emergence in Life Sciences.

ISBN p. ^ Bonabeau, Eric; Dorigo, Marco and Theraulaz, Guy (). Swarm intelligence: from natural to artificial systems.

The mapping of sequence (genotype) into structure (phenotype) has been shown to be tractable in RNA and also in proteins and has three fundamental properties: (i) there are many more sequences than structures (i.e.

the sequence-to-structure map is highly degenerate); (ii) few common, but many rare, structures materialize in structure space; and Cited by: We have developed a new nanotagging technology for detecting and imaging the self-organization of proteins and other components of membranes at nanometer resolution for the purpose of investigating cell signaling and other membrane-mediated biological processes.

We used protein- lipid- or drug. In enzyme proteins, cold adaptation is attained through functional trade-offs between stability and activity, often mediated by substitutions outside the active site. Little is known whether signaling proteins [e.g., G protein-coupled receptors (GPCRs)] exhibit natural variation in response to cold temperatures.

The Raw Materials: Biomolecular Structure and Stability Molecules are composed of atoms linked by covalent bonds Globular proteins have a hierarchical structure Stable globular structure requires a combination of design strategies Self-Organization Lipids self-organize into bilayers.

Proteins are subject to various conflicting forces that trade-off against each other. For example, during folding, the protein achieves lower enthalpy at the cost of lower entropy.

Similarly, the trade-off for increased stability may be decreased flexibility, which may abolish allosteric pathways. The fuzzy oil drop model, a tool which can be used to study the structure of the hydrophobic core in proteins, has been applied in the analysis of proteins belonging to the jumonji group—JARID2, JARID1A, JARID1B and JARID1D—proteins that share the property of being able to interact with DNA.

Their ARID and PHD domains, when analyzed in the context of the fuzzy oil drop model, are found to Cited by: A food web (or food cycle) is the natural interconnection of food chains and a graphical representation (usually an image) of what-eats-what in an ecological r name for food web is consumer-resource ists can broadly lump all life forms into one of two categories called trophic levels: 1) the autotrophs, and 2) the heterotrophs.

Introduction. Despite the classical structure-function paradigm (which is typically envisioned as the “lock-and-key” model, in which a unique biological function of a protein is defined by its specific, highly structured state determined by the amino acid sequence []) that dominated scientific minds for more than a century, many protein functions do not require a unique by: This book gives an overview of the methods and results obtained so far by studying the characteristics and properties of nanoscale self-organized networks.

It demonstrates the universality of the network approach over a range of disciplines, from protein folding to the newest electronic materials. basic self-organization events are modulated by the crowded interior of live cells.

To find out, we use here in-cell NMR to follow book illustrations, some proteins are tuned to work at marginal structural stability.

The advantage of such tuning is that thus that proteins are optimized not only for structure and func-Cited by:. Book Reviews Biological Membranes: Structure, studies have shown that protein self-organization is an autonomous and 'stability' is only discussed in connection with the role of Author: Rainer Jaenicke.Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food industries, in addition to being a daily consideration for academic researchers studying proteins.

An understanding of protein stability is essential for optimizing the expression, purification, formulation, storage and structural studies of proteins.Matthias J.

Feige, Ineke Braakman and Linda M. Hendershot, CHAPTER Disulfide Bonds in Protein Folding and Stability, in Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering,pp. DOI: / eISBN: