GLORIA

GEOMAR Library Ocean Research Information Access

X
Language
Preferred search index
Number of Hits per Page
Default Sort Criterion
Default Sort Ordering
Size of Search History
Default Email Address
Default Export Format
Default Export Encoding
Facet list arrangement
Maximum number of values per filter
Auto Completion
Topics (search only within journals and journal articles that belong to one or more of the selected topics)
Show more topics
Feed Format
Maximum Number of Items per Feed
Permalink If you want to be able to use settings permanently, you must save your settings and then set a Bookmark to the permalink
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 2000-2004  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Mechanisms of cooperativity underlying sequence-independent β-sheet formation (2002)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 116 (2002), S. 4353-4365 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We investigate the formation of β-sheet structures in proteins without sequence-dependent side-chain interactions. To accomplish this, we introduce a model which explicitly incorporates both solvation effects and the angular dependence (on the protein backbone) of hydrogen bond formation. The thermodynamics of this model is studied by exploring the density of states for the entire system and the local couplings in a partially folded structure. Our results suggest that solvation dynamics together with the H-bond angular dependence gives rise to a generic cooperativity in this class of systems; this result explains why pathological aggregates involving β-sheet cores can form from many different proteins. Our work provides the foundation for the construction of phenomenological models to investigate topology effects in β-sheet folding and the competition between native folding and nonspecific aggregation. © 2002 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1448493
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The artistry of nature (2001)
    [s.l.] : Nature Publishing Group
    Nature 409 (2001), S. 985-986 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ...The endless array of patterns and shapes in nature has long been a source of joy and wonder to laymen and scientists alike. Discovering how such patterns emerge spontaneously from an orderless and homogeneous environment has been a challenge to researchers in the natural sciences throughout the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35059178
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A Statistical Mechanics Model for Receptor Clustering (2000)
    Springer
    Journal of biological physics 26 (2000), S. 219-234 
    Details
    ISSN: 1573-0689
    Keywords: Signal transduction ; Receptor clustering ; Statistical mechanics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract We introduce and study a simple lattice statistical mechanics modelfor the clustering of tumor necrosis factor receptor I (TNFR1).Our model explains clustering under over-expression of the cytoplasmicsignal transducer as well as the clustering induced via extracellularligand binding; also we explain why the loss of transducer leads to arapid break-up of the clusters. The basic mechanism at work is a first-order(cooperative) phase transition caused by the multimeric binding capability ofthe receptor-transducer complex. Using cooperativity of this type, the cellsare found to have an enhanced sensitivity and robustness. In general, ourmethod can be applied to other receptor-clustering related signaling system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1010313529687
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...