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Principles of protein-protein interactions.

TLDR
Property such as sequence conservation and co-regulation of genes and proteins involved in different types of physical interactions are discussed, given that all proteins consist of their evolutionary units, the domains, all interactions occur between these domains.
Abstract
In the postgenomic era, one of the most interesting and important challenges is to understand protein interactions on a large scale. The physical interactions between protein domains are fundamental to the workings of a cell: in multi-domain polypeptide chains, in multi-subunit proteins and in transient complexes between proteins that also exist independently. Thus experimental investigation of protein-protein interactions has been extensive, including recent large-scale screens using mass spectrometry. The role of computational research on protein-protein interactions encompasses not only prediction, but also understanding the nature of the interactions and their three-dimensional structures. I will discuss properties such as sequence conservation and co-regulation of genes and proteins involved in different types of physical interactions. Given that all proteins consist of their evolutionary units, the domains, all interactions occur between these domains. The interactions between domains belonging to different protein families will be the second topic of my talk.

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Journal ArticleDOI

Reaching for high-hanging fruit in drug discovery at protein–protein interfaces

TL;DR: These studies discovered small molecules that bind with drug-like potencies to 'hotspots' on the contact surfaces involved in protein–protein interactions, and bind with much higher efficiencies than do the contact atoms of the natural protein partner.
Journal ArticleDOI

Water mediation in protein folding and molecular recognition

TL;DR: Focusing on water sheds light on the physics and function of biological machinery and self-assembly and may advance the understanding of the natural design of proteins and nucleic acids.
Journal ArticleDOI

PIPER: An FFT‐based protein docking program with pairwise potentials

TL;DR: The Fast Fourier Transform correlation approach to protein–protein docking is efficiently used with pairwise interaction potentials that substantially improve the docking results, and a novel class of structure‐based pairwise intermolecular potentials are presented.
Journal ArticleDOI

High-affinity binders selected from designed ankyrin repeat protein libraries.

TL;DR: The evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding and combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces are generated, an attractive alternative to antibody libraries.
Journal ArticleDOI

Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains

TL;DR: A comparative analysis of the structural relationships among vertebrate PTP domains is presented and a comprehensive resource for sequence analysis of phosphotyrosine-specific PTPs is provided.
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