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Analyzing the effect of homogeneous frustration in protein folding
(2013-10-01)
The energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy ...
Analyzing the effect of homogeneous frustration in protein folding
(2013-10-01)
The energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy ...
Ab initio protein folding simulations using atomic burials as informational intermediates between sequence and structure
(Wiley-Blackwell, 2014-07-01)
The three-dimensional structure of proteins is determined by their linear amino acid sequences but decipherment of the underlying protein folding code has remained elusive. Recent studies have suggested that burials, as ...
Thioredoxin from Escherichia coli as a role model of molecular recognition, folding, dynamics and function
(Bentham Science Publishers, 2015-09)
Thioredoxin (TRX) catalyzes redox reactions via the reversible oxidation of the conserved active center CGPC and it is involved in multiple biological processes, some of them linked to redox activity while others not. TRX ...
Structural characteristics of the TPR Protein-Hsp90 interaction: A new target in biotechnology
(Bentham Science Publishers, 2018)
Nature employs multiple repeat protein scaffolds in order to promote proteinprotein interactions. In this sense, TPR proteins participate in different natural pathways, especially in diverse processes of eukaryotic cells. ...
Structural basis of molecular recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at membrane surfaces
(Elsevier, 2011)
The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stageregulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania ...
The Design of Repeat Proteins: Stability Conflicts with Functionality
(Insight Medical Publishing, 2017-03)
Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces ...
Frustration, function and folding
(Current Biology, 2018-02-05)
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, ...