Results 11 to 20 of about 13,117,352 (339)

Protein [PDF]

open access: yesAdvances in Nutrition, 2011
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
openaire   +5 more sources

Proteins, proteins everywhere [PDF]

open access: yesScience, 2021
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.
openaire   +2 more sources

Contextualized Protein-Protein Interactions [PDF]

open access: yesPatterns, 2021
Protein-protein interaction (PPI) databases are an important bioinformatics resource, yet existing literature-curated databases usually represent cell-type-agnostic interactions, which is at variance with our understanding that protein dynamics are context specific and highly dependent on their environment.
Anthony Federico, Stefano Monti
openaire   +4 more sources

Protein–protein interactions

open access: yesCurrent Opinion in Structural Biology, 2013
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 ...
Joël Janin, Alexandre M. J. J. Bonvin
openaire   +4 more sources

Bacteriophage Protein–Protein Interactions [PDF]

open access: yes, 2012
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
Roman Häuser   +9 more
openaire   +5 more sources

INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]

open access: yesBiocomputing 2012, 2011
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 ...
Bin Xue   +7 more
openaire   +4 more sources

How proteins bind macrocycles [PDF]

open access: yes, 2014
The potential utility of synthetic macrocycles (MCs) as drugs, particularly against low-druggability targets such as protein-protein interactions, has been widely discussed. There is little information, however, to guide the design of MCs for good target
Beglov, Dmitri   +6 more
core   +1 more source

Protein–Protein and Protein–Membrane Associations in the Lignin Pathway [PDF]

open access: yesThe Plant Cell, 2012
Supramolecular organization of enzymes is proposed to orchestrate metabolic complexity and help channel intermediates in different pathways. Phenylpropanoid metabolism has to direct up to 30% of the carbon fixed by plants to the biosynthesis of lignin precursors. Effective coupling of the enzymes in the pathway thus seems to be required.
Bassard, Jean-Etienne   +13 more
openaire   +5 more sources

Why Do Proteins Look Like Proteins?

open access: yes, 1996
Protein structures in nature often exhibit a high degree of regularity (secondary structures, tertiary symmetries, etc.) absent in random compact conformations.
Helling, Robert   +3 more
core   +1 more source

Morphology of protein–protein interfaces [PDF]

open access: yesStructure, 1998
Most soluble proteins are active as low-number oligomers. Statistical surveys of oligomeric proteins have defined the roles of hydrophobicity and complementarity in the stability of protein interfaces, but tend to average structural features over a diverse set of protein-protein interfaces, blurring information on how individual interfaces are ...
David S. Goodsell   +2 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy