dorsal/arxiv
View SchemaA Structure-Centric View of Protein Evolution, Design and Adaptation
| Authors | Eric J. Deeds, Eugene I. Shakhnovich |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0603028 |
| URL | https://arxiv.org/abs/q-bio/0603028 |
Abstract
Proteins, by virtue of their central role in most biological processes, represent one of the key subjects of the study of molecular evolution. Inherent to the indispensability of proteins for living cells is the fact that a given protein can adopt a specific three-dimensional shape that is specified solely by the proteins sequence of amino acids. Over the past several decades, structural biologists have demonstrated that the array of structures that proteins may adopt is quite astounding, and this has lead to a strong interest in understanding how protein structures change and evolve over time. In this review we consider a large body of recent work that attempts to illuminate this structure-centric picture of protein evolution. Much of this work has focused on the question of how completely new protein structures (i.e. new folds or topologies) are discovered by protein sequences as they evolve. Pursuant to this question of structural innovation has been a desire to describe and understand the observation that certain types of protein structures are far more abundant than others and how this uneven distribution of proteins implicates on the process through which new shapes are discovered. We consider a number of theoretical models that have been successful at explaining this heterogeneity in protein populations and discuss the increasing amount of evidence that indicates that the process of structural evolution involves the divergence of protein sequences and structures from one another.
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"abstract": "Proteins, by virtue of their central role in most biological processes,\nrepresent one of the key subjects of the study of molecular evolution. Inherent\nto the indispensability of proteins for living cells is the fact that a given\nprotein can adopt a specific three-dimensional shape that is specified solely\nby the proteins sequence of amino acids. Over the past several decades,\nstructural biologists have demonstrated that the array of structures that\nproteins may adopt is quite astounding, and this has lead to a strong interest\nin understanding how protein structures change and evolve over time. In this\nreview we consider a large body of recent work that attempts to illuminate this\nstructure-centric picture of protein evolution. Much of this work has focused\non the question of how completely new protein structures (i.e. new folds or\ntopologies) are discovered by protein sequences as they evolve. Pursuant to\nthis question of structural innovation has been a desire to describe and\nunderstand the observation that certain types of protein structures are far\nmore abundant than others and how this uneven distribution of proteins\nimplicates on the process through which new shapes are discovered. We consider\na number of theoretical models that have been successful at explaining this\nheterogeneity in protein populations and discuss the increasing amount of\nevidence that indicates that the process of structural evolution involves the\ndivergence of protein sequences and structures from one another.",
"arxiv_id": "q-bio/0603028",
"authors": [
"Eric J. Deeds",
"Eugene I. Shakhnovich"
],
"categories": [
"q-bio.BM",
"q-bio.PE"
],
"title": "A Structure-Centric View of Protein Evolution, Design and Adaptation",
"url": "https://arxiv.org/abs/q-bio/0603028"
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