Results 301 to 310 of about 6,229,094 (322)

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
Sandor Vajda, Carlos J. Camacho
openaire   +3 more sources

The impact of protein flexibility on protein–protein docking

Proteins: Structure, Function, and Bioinformatics, 2004
AbstractAccounting 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, Lutz P. Ehrlich, Michael Nilges   +2 more
openaire   +3 more sources

Protein-Protein Interactions in Membranes

Protein & Peptide Letters, 2011
In 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., Sandqvist, E., Rheinstädter, M.C.   +2 more
openaire   +3 more sources

DISCOVERING PROTEIN–PROTEIN INTERACTIONS

Journal of Bioinformatics and Computational Biology, 2004
The ongoing genomics and proteomics efforts have helped identify many new genes and proteins in living organisms. However, simply knowing the existence of genes and proteins does not tell us much about the biological processes in which they participate. Many major biological processes are controlled by protein interaction networks.
See-Kiong Ng, Soon-Heng Tan
openaire   +2 more sources

Protein Phosphorylation and Protein-Protein Interactions

2002
Intracellular signaling is the series of events which translates the specific message of circulating ligands into a particular biological response in target cells. The first step in hormone signaling involves the interaction between a ligand and its cognate receptor (membrane or nuclear), which in turn induces stoichiometric and conformational changes ...
Paul A. Kelly, Vincent Goffin
openaire   +2 more sources

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.
openaire   +3 more sources

Protein–protein interactions of KChIP proteins and Kv4.2

Biochemical and Biophysical Research Communications, 2004
To prove heteromeric assembly of KChIP proteins, the present study is carried out. The results of chemical crosslinking and pull down assay revealed that KChIP1, KChIP2.1, and KChIP2.2 could form homo- as well as hetero-oligomer, and this oligomerization exhibited a Ca(2+)-dependent manner. Moreover, homomeric and heteromeric assembly of KChIPs did not
Ching-Ping Cheng, Long-Sen Chang, Ya-Ling Lin, Chia-Yi Chen   +3 more
openaire   +3 more sources

Protein-protein interactions

1990
International ...
Popineau, Yves, Feillet, P.
openaire   +3 more sources

Protein recruitment systems for the analysis of protein–protein interactions

Biochemical Pharmacology, 2000
The yeast Saccharomyces cerevisiae serves as an excellent genetic tool for the analysis of protein +/- protein interactions. The most common system, used to date, is the two-hybrid system. Although proven very powerful, the two-hybrid system exhibits several inherent problems and limitations.
openaire   +4 more sources

Osmolytes and Protein–Protein Interactions

Journal of the American Chemical Society, 2018
Cells survive fluctuations in osmolality by accumulating and depleting highly soluble, usually neutral, small organic compounds. Natural selection has converged on a small set of such molecules, called osmolytes. The biophysical characterization of osmolytes, with respect to proteins, has centered on tertiary structure stability.
Amy E. Rydeen, Eric M. Brustad, Gary J. Pielak   +2 more
openaire   +4 more sources