Results 311 to 320 of about 12,507,251 (357)

Protein-catalysed protein folding

Trends in Biotechnology, 1990
A number of proteins, termed chaperonins, have been identified as part of the mechanism of folding other proteins into their biologically active forms. The role of chaperonins appears to be twofold--to prevent illegitimate interactions with other proteins and to facilitate folding, possibly through an energy-dependent, catalytic function.
A L, Horwich, W, Neupert, F U, Hartl
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Protein myristoylation in protein–lipid and protein–protein interactions

Biophysical Chemistry, 1999
Various 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 ...
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Measuring protein—protein interactions

Current Opinion in Structural Biology, 1998
The binding of one protein to another provokes a variety of biophysical changes that can then be used as a measure of the binding reaction. Optical spectroscopy, particularly fluorescence, is the most flexible technique, but surface plasmon resonance biosensors, microcalorimetry and mass spectroscopy have recently shown significant development.
J H, Lakey, E M, Raggett
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Protein-Protein Interactions

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.
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Proteine, Proteine

forschung, 2018
AbstractSonja Lorenz erforscht das in allen Körperzellen wirksame Ubiquitinsystem.
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Designed Protein-Protein Association

Science, 2008
The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface.
Dirk, Grueninger, Nora, Treiber, Mathias O P, Ziegler, Jochen W A, Koetter, Monika-Sarah, Schulze, Georg E, Schulz   +5 more
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Protein–protein association kinetics and protein docking

Current Opinion in Structural Biology, 2002
Rigid 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
Carlos J, Camacho, Sandor, Vajda
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Protein–Protein Interaction Regulates Proteins’ Mechanical Stability

Journal of Molecular Biology, 2008
Elastomeric proteins are molecular springs found not only in a variety of biological machines and tissues, but also in biomaterials of superb mechanical properties. Regulating the mechanical stability of elastomeric proteins is not only important for a range of biological processes, but also critical for the use of engineered elastomeric proteins as ...
Yi, Cao, Teri, Yoo, Shulin, Zhuang, Hongbin, Li   +3 more
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Correlating Protein–DNA and Protein–Protein Interaction Networks

Journal of Molecular Biology, 2003
Here, we search protein-DNA binding data for prevalent pairs and higher-order tuples of co-occurring transcription factors (TF) in Saccharomyces cerevisiae. While the identification of such modules is dependent on uncertainties of genome-wide data sets, we find several biologically meaningful examples, which allow putative annotation of yet ...
Manke, T., Bringas, R., Vingron, M.
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Protein-Protein Interaction Databases

2015
Years of meticulous curation of scientific literature and increasingly reliable computational predictions have resulted in creation of vast databases of protein interaction data. Over the years, these repositories have become a basic framework in which experiments are analyzed and new directions of research are explored.
Szklarczyk, Damian, Jensen, Lars Juhl
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