Publication

Protein de novo design: Macromolecules with tailormade properties

1996
Journal Articles

Abstract

In the absence of a detailed knowledge of the folding mechanism of natural proteins, the general design of polypeptide sequences with a high propensity to fold into a predetermined three dimensional structure still appears to be out of reach. The concept of Template Assembled Synthetic Proteins (TASP) represents a means by which one call nonetheless construct macromolecules with native-like structural features, with the result that systems with tailormade structural and functional properties are non becoming attainable.

Official source

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

1996
Journal Articles

Abstract

Official source

Related concepts (32)

Protein engineering

Protein engineering is the process of developing useful or valuable proteins through the design and production of unnatural polypeptides, often by altering amino acid sequences found in nature. It is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles. It has been used to improve the function of many enzymes for industrial catalysis. It is also a product and services market, with an estimated value of $168 billion by 2017.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Structural bioinformatics

Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds and local motifs, principles of molecular folding, evolution, binding interactions, and structure/function relationships, working both from experimentally solved structures and from computational models.

Related publications (4)

Protein de novo design: Macromolecules with tailormade properties

Chat with Graph Search

Design of lattice proteins with explicit solvent

Surface grafting onto template-assembled synthetic protein scaffolds in molecular recognition

Formation of stable polypeptide monolayers at interfaces: controlling molecular conformation and orientation