Výsledky vyhledávání - "partial unfolding"

Akademický článek

Folding and Stability of Ankyrin Repeats Control Biological Protein Function

Autor: Amit Kumar, Jochen Balbach

Publikováno v: Biomolecules, Vol 11, Iss 6, p 840 (2021)

Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repea

Externí odkaz: https://doaj.org/article/29e828ac9a764e948c824e901a586b1f

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Akademický článek

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Akademický článek

Multiple-Basin Energy Landscapes for Large-Amplitude Conformational Motions of Proteins: Structure-Based Molecular Dynamics Simulations

Autor: Okazaki, Kei-ichi, Koga, Nobuyasu, Takada, Shoji, Onuchic, Jose N., Wolynes, Peter G.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 2006 Aug 01. 103(32), 11844-11849.

Externí odkaz: https://www.jstor.org/stable/30051628

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Folding and Stability of Ankyrin Repeats Control Biological Protein Function

Autor: Jochen Balbach, Amit Kumar

Publikováno v: Biomolecules, Vol 11, Iss 840, p 840 (2021)
Biomolecules

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee03cc9c1d28965a5e5e904b5c9942cb
https://doi.org/10.3390/biom11060840

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Mechanism of inactivation of ocriplasmin in porcine vitreous

Autor: Bernard Noppen, Marc D. de Smet, Rita Derua, Marc Vanhove, F. Aerts, Etienne Waelkens, Laetitia Fonteyn

Publikováno v: Biophysical chemistry.

Ocriplasmin, a 249-amino acid recombinant C-terminal fragment of human plasmin, has the potential to degrade, within the eye, the protein scaffold that links the vitreous to the retina. This may be beneficial to the treatment of a number of important

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f94cf3b3cfbf878d258fce35342ca3d
https://pubmed.ncbi.nlm.nih.gov/22445213

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Akademický článek

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Dissertation/ Thesis

The Folding Energy Landscape of MerP

Autor: Brorsson, Ann-Christin

This thesis is based on studies, described in four papers, in which the folding energy landscape of MerP was investigated by various techniques. MerP is a water-soluble 72 amino acid protein with a secondary structure consisting of four anti-parallel

Externí odkaz: http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-309

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Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity

Autor: Stefania, Iametti, Patrizia, Rasmussen, Hanne, Frøkiaer, Pasquale, Ferranti, Francesco, Addeo, Francesco, Bonomi

Publikováno v: 269 (2002): 1362–1372.
info:cnr-pdr/source/autori:Iametti S., Rasmussen P., Frokiaer H., Ferranti P., Addeo F., Bonomi F./titolo:Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity/doi:/rivista:/anno:2002/pagina_da:1362/pagina_a:1372/intervallo_pagine:1362–1372/volume:269

Bovine beta-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65 degrees C at neutral pH. At these temperatures beta-lactoglobulin undergoes significant but reversible structural changes. In the c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0da3ca11a7971c3dd65224a5ea821fa4
https://publications.cnr.it/doc/45525

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