Results 11 to 20 of about 7,411,435 (267)
Proteins, proteins everywhere [PDF]
The first protein structures were determined by x-ray crystallography in 1957 by John C. Kendrew and Max F. Perutz. As a bioinorganic chemist, I was delighted that the structures were myoglobin and hemoglobin, both heme proteins with big, beautiful iron atoms.
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INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]
Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun Hsu +7 more
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Modulators of Protein–Protein Interactions [PDF]
No ...
Milroy, L. +4 more
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Protein-protein interaction prediction for targeted protein degradation [PDF]
Abstract Protein-protein interactions (PPIs) play a fundamental role in various biological functions; thus, detecting PPI sites is essential for understanding diseases and developing new drugs. PPI prediction is of particular relevance for the development of drugs employing targeted protein degradation, as their efficacy relies on the ...
Oliver Orasch +5 more
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Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System [PDF]
Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and Hsp90. It is enigmatic how these machines fold proteins.
Mayer, Matthias +5 more
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Bacteriophage Protein–Protein Interactions [PDF]
Bacteriophages T7, λ, P22, and P2/P4 (from Escherichia coli), as well as ϕ29 (from Bacillus subtilis), are among the best-studied bacterial viruses. This chapter summarizes published protein interaction data of intraviral protein interactions, as well as known phage-host protein interactions of these phages retrieved from the literature. We also review
Häuser, R. +8 more
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Picky Hsp90-Every Game with Another Mate [PDF]
In this issue of Molecular Cell, Sahasrabudhe et al. (2017) present a dramatically renovated functional cycle for the molecular chaperone Hsp90, which stimulates re-thinking of the mechanism of this vital protein folding ...
Sub Cellular Protein Chemistry +3 more
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We are proud to present the first edition of the Protein–protein interactions Section of Current Opinion in Structural Biology. The Section is new, but the topic has been present in the journal from the very start. Volume 1, Issue 1, dated February 1991, had a review by Janin entitled Protein–protein interactions and assembly, and others by Bode and ...
Janin, Joel, Bonvin, Alexandre M. J. J.
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Analysis of Disulfide Bond Formation [PDF]
In this unit, protocols are provided for detection of disulfide bond formation in cultures of intact cells and in an in vitro translation system containing isolated microsomes or semi-permeabilized cells.
Sub Cellular Protein Chemistry +9 more
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Proteins are polymers of amino acids linked via α-peptide bonds. They can be represented as primary, secondary, tertiary, and even quaternary structures, but from a nutritional viewpoint only the primary (amino acid) sequence is of interest. Similarly, although there are many compounds in the body that can be chemically defined as amino acids, we are ...
Malcolm, Watford, Guoyao, Wu
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