2I1345 Simplified amino acid sequences that fold into native structures
نویسندگان
چکیده
منابع مشابه
Design of amino acid sequences to fold into C(alpha)-model proteins.
In order to extend the results obtained with minimal lattice models to more realistic systems, we study a model where proteins are described as a chain of 20 kinds of structureless amino acids moving in a continuum space and interacting through a contact potential controlled by a 20x20 quenched random matrix. The goal of the present work is to design and characterize amino acid sequences foldin...
متن کاملProtein Tertiary Structures: Prediction from Amino Acid Sequences
Proteins are polypeptide chains consisting of a large number of amino acid residues that are covalently linked together via amide bonds. The order in which the 20 different amino acids are arranged in a protein chain is also called the primary structure of the protein. The polypeptide backbones of proteins exist in particular conformations known as the secondary structures. The secondary struct...
متن کاملSimplified amino acid alphabets for protein fold recognition and implications for folding.
Protein design experiments have shown that the use of specific subsets of amino acids can produce foldable proteins. This prompts the question of whether there is a minimal amino acid alphabet which could be used to fold all proteins. In this work we make an analogy between sequence patterns which produce foldable sequences and those which make it possible to detect structural homologs by align...
متن کاملAmino acid distribution rules predict protein fold.
In the present article, we provide a brief overview of the main approaches to analysing the sequence-structure relationship of proteins and outline a novel method of structure prediction. The proposed method involves finding a set of rules that describes a correlation between the distribution of residues in a sequence and the essential structural characteristics of a protein structure. The resi...
متن کاملOrientational potentials extracted from protein structures improve native fold recognition.
We develop coarse-grained, distance- and orientation-dependent statistical potentials from the growing protein structural databases. For protein structural classes (alpha, beta, and alpha/beta), a substantial number of backbone-backbone and backbone-side-chain contacts stabilize the native folds. By taking into account the importance of backbone interactions with a virtual backbone interaction ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2002
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.42.s122_3