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Amino acid repeat patterns in protein sequences: Their diversity and structural‐functional implications

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TLDR
It appears that repeated sequence patterns may be a mechanism that provides regular arrays of spatial and functional groups, useful for structural packing or for one to one interactions with target molecules.
Abstract
All the protein sequences from SWISS-PROT database were analyzed for occurrence of single amino acid repeats, tandem oligo-peptide repeats, and periodically conserved amino acids. Single amino acid repeats of glutamine, serine, glutamic acid, glycine, and alanine seem to be tolerated to a considerable extent in many proteins. Tandem oligo-peptide repeats of different types with varying levels of conservation were detected in several proteins and found to be conspicuous, particularly in structural and cell surface proteins. It appears that repeated sequence patterns may be a mechanism that provides regular arrays of spatial and functional groups, useful for structural packing or for one to one interactions with target molecules. To facilitate further explorations, a database of Tandem Repeats in Protein Sequences (TRIPS) has been developed and is available at URL: http://www.ncl-india.org/trips.

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Differential Distribution of Simple Sequence Repeats in Eukaryotic Genome Sequences

TL;DR: Analysis of complete genome coding DNA sequences of Drosophila, C. elegans, and yeast indicated that expansions of codon repeat corresponding to small hydrophilic amino acids are tolerated more, while strong selection pressures probably eliminate codon repeats encoding hydrophobic and basic amino acids.
Journal ArticleDOI

Simple sequence repeats as advantageous mutators in evolution.

TL;DR: These studies support the hypothesis that SSRs, by virtue of their special mutational and functional qualities, have a major role in generating the genetic variation underlying adaptive evolution.
Journal ArticleDOI

Microsatellite markers: what they mean and why they are so useful.

TL;DR: This review aims to address some theoretical aspects of SSRs, including definition, characterization and biological function, and confirms the current relevance ofSSRs and indicates their continuous utilization in plant science.
Journal ArticleDOI

The UL6 Gene Product Forms the Portal for Entry of DNA into the Herpes Simplex Virus Capsid

TL;DR: The results are interpreted to support the view that pUL6 forms the DNA entry portal, since it exists at a unique site in the capsid and forms a channel through which DNA can pass, and suggests the basic mechanism of DNA packaging is conserved.
Journal ArticleDOI

Tandem repeats in proteins: from sequence to structure.

TL;DR: Appraisal of the known structures and their classification uncovers a straightforward relationship between their architecture and the length of the repetitive units and this relationship and the repetitive character of structural folds suggest rules for better prediction of the 3D structures of such proteins.
References
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Journal ArticleDOI

The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
Journal ArticleDOI

The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999.

TL;DR: The Human Proteomics Initiative (HPI), a major project to annotate all known human sequences according to the quality standards of SWISS-PROT, is described.
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The SWISS-PROT protein sequence data bank and its supplement TrEMBL

TL;DR: This supplement consists of entries in SWiss-PROT-like format derived from the translation of all coding sequences in the EMBL nucleotide sequence database, except the CDS already included in SWISS- PROT.
Journal ArticleDOI

Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases

TL;DR: Molecular modeling followed by optical, electron, and x-ray diffraction studies of a synthetic poly(L-glutamine) shows that it forms beta-sheets strongly held together by hydrogen bonds.
Journal ArticleDOI

Transcriptional activation modulated by homopolymeric glutamine and proline stretches.

TL;DR: Many transcription factors contain proline- or glutamine-rich activation domains and it is shown that simple homopolymeric stretches of these amino acids can activate transcription when fused to the DNA binding domain of GAL4 factor.
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