Results 281 to 290 of about 13,117,352 (339)
Some of the next articles are maybe not open access.
Biochemical Society Transactions, 2010
In the present article, we describe the two standard high-throughput methods for identification of protein complexes: two-hybrid screens and TAP (tandem affinity purification) tagging. These methods have been used to characterize the interactome of Saccharomyces cerevisiae, showing that the majority of proteins are part of complexes, and that complexes
Williamson, Mike P. +1 more
openaire +4 more sources
In the present article, we describe the two standard high-throughput methods for identification of protein complexes: two-hybrid screens and TAP (tandem affinity purification) tagging. These methods have been used to characterize the interactome of Saccharomyces cerevisiae, showing that the majority of proteins are part of complexes, and that complexes
Williamson, Mike P. +1 more
openaire +4 more sources
Analysis of Protein-Protein Interactions by Protein Microarrays
2021The analysis of the proteome and the interactome would be useful for a better understanding of the pathophysiology of several disorders, allowing the identification of potential specific markers for early diagnosis and prognosis, as well as potential targets of intervention.
Rodrigo Barderas, Ana Montero-Calle
openaire +3 more sources
Protein myristoylation in protein–lipid and protein–protein interactions
Biophysical Chemistry, 1999Various proteins in signal transduction pathways are myristoylated. Although this modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification exerts its effects is still largely unknown. Here we discuss the roles played by protein myristoylation, in both protein-lipid and protein-protein ...
openaire +3 more sources
Protein–protein association kinetics and protein docking
Current Opinion in Structural Biology, 2002Rigid body protein docking methods frequently yield false positive structures that have good surface complementarity, but are far from the native complex. The main reason for this is the uncertainty of the protein structures to be docked, including the positions of solvent-exposed sidechains. Substantial efforts have been devoted to finding near-native
Sandor Vajda, Carlos J. Camacho
openaire +3 more sources
The impact of protein flexibility on protein–protein docking
Proteins: Structure, Function, and Bioinformatics, 2004AbstractAccounting for protein flexibility in protein–protein docking algorithms is challenging, and most algorithms therefore treat proteins as rigid bodies or permit side‐chain motion only. While the consequences are obvious when there are large conformational changes upon binding, the situation is less clear for the modest conformational changes ...
Rebecca C. Wade +2 more
openaire +3 more sources
1954
Publisher Summary This chapter focuses on protein–protein interaction. The unique characteristics of different proteins are developed in the interactions of proteins with each other, with ions, and with nonprotein materials such as lipids, nucleic acids, and carbohydrates.
openaire +3 more sources
Publisher Summary This chapter focuses on protein–protein interaction. The unique characteristics of different proteins are developed in the interactions of proteins with each other, with ions, and with nonprotein materials such as lipids, nucleic acids, and carbohydrates.
openaire +3 more sources
Protein-Protein Interactions in Membranes
Protein & Peptide Letters, 2011In this article we review the current status of our understanding of membrane mediated interactions from theory and experiment. Phenomenological mean field and molecular models will be discussed and compared to recent experimental results from dynamical neutron scattering and atomic force microscopy.
Armstrong, C.L. +2 more
openaire +3 more sources