Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Frauke Graeter"'
Publikováno v:
Biophysical Journal. 108(2)
Spider dragline silk, solely made from protein, outperforms synthetic fibers in terms of toughness and extensibility, which is thought to originate from its refined nano-scale hierarchical structure. The key for understanding the outstanding mechanic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7461437398b98700f574f231adff7272
Publikováno v:
Biophysical Journal. 110:323a
Disordered proteins have the capacity to self-assemble from random coils to partial or complete folded structures. Such combination of amorphous/ordered phases within the protein structure is determined by the aminoacid sequence as well as enviroment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e314756d8cc18d650f931f0c8ef28336
https://doi.org/10.1016/j.bpj.2015.11.1736
https://doi.org/10.1016/j.bpj.2015.11.1736
Autor:
Ilona B. Baldus, Frauke Graeter
Publikováno v:
Biophysical Journal. 100(3)
Mechanical pulling forces have been shown to significantly alter the rate of redox reactions in various thiol/disulfide exchange systems [1]. However, it has been questioned if force can directly affect the electron affinity of such redox systems [2]
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97de7b2b841fd8cf923efbd7558ac265
Publikováno v:
Biophysical Journal. 100(3)
Silk is an intriguing protein-based material that combines elasticity and strength to an extent not yet reached by any synthetic material today. Silk fibers are composed of highly-ordered beta-sheet crystals and an amorphous peptide matrix that both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::520d2df109fdc80e5b944d43326bc506
Publikováno v:
Biophysical Journal. 102:251a-252a
Protein folds have been invented and adopted under various evolutionary constraints. The question arises how general mechanical attributes that control protein function have been sampled by the evolving protein domain repertoire in the varying biolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78023c9a7f1727f0ea88ee61d8434057
https://doi.org/10.1016/j.bpj.2011.11.1387
https://doi.org/10.1016/j.bpj.2011.11.1387
Publikováno v:
Biophysical Journal. 98:632a-633a
ADAMTS13 is a plasma zinc metalloproteinase crucial for primary haemostasis, the enzymatic activity of which is biomechanically controlled. Shear stress-induced partial unfolding of its substrate, the von Willebrand factor (vWF) A2 domain, is essenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a63c8bd161af96f899c7d83a5b9ae29
https://doi.org/10.1016/j.bpj.2009.12.3463
https://doi.org/10.1016/j.bpj.2009.12.3463
Publikováno v:
Biophysical Journal. 102:735a
Regulation of (Bio)chemical reactions by mechanical force has been proposed to be fundamental to cellular functions[1]. Atomic force microscopy and molecular force probe experiments suggested an enhancement on the reactivity of thiol/disulfide exchan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d71a21d47692405fa2a3551e2d668bf4
https://doi.org/10.1016/j.bpj.2011.11.3987
https://doi.org/10.1016/j.bpj.2011.11.3987
Publikováno v:
Biophysical Journal. 98:596a
Single-molecule measurements of how proteins respond to applied force can provide valuable clues to their structure-function relationship, particularly for proteins whose role in vivo relies on an ability to resist or sense force. Interpretation of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bbbd59ca7ed58b9b7d2e4c1f9c2d21d
https://doi.org/10.1016/j.bpj.2009.12.3243
https://doi.org/10.1016/j.bpj.2009.12.3243
Autor:
Wolfram Stacklies, Frauke Graeter
Publikováno v:
Biophysical Journal. 96:589a
Mechanical force is routinely applied to proteins in force probing experiments and simulations to observe a protein's response to external stress. A yet unanswered question is how force propagates through proteins. How do perturbations like an extern
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d46796e2cf276ef4001c1abface80e0d
https://doi.org/10.1016/j.bpj.2008.12.3087
https://doi.org/10.1016/j.bpj.2008.12.3087
Autor:
Antje Pieconka, Ulrich Budde, Sonja Schneppenheim, Tobias Obser, Carsten Baldauf, Reinhard Schneppenheim, Frauke Graeter
Publikováno v:
Blood. 112:589-589
Background: An important regulatory mechanism of VWF functional activity is the proteolysis of the VWF high molecular weight multimers by ADAMTS13. The ADAMTS13 specific proteolytic site is located in the VWF A2 domain between Y1605 and M1606. Homolo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb428a60f68b2ebd1f5f3e155c3fa978
https://doi.org/10.1182/blood.v112.11.589.589
https://doi.org/10.1182/blood.v112.11.589.589