ArticleInternational journal of molecular sciences2019
Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- RNA-Binding S1 Domain in Bacterial, Archaeal and Eukaryotic Proteins as One of the Evolutionary Markers of Symbiogenesis.International journal of molecular sciences · 2024Article
- Diversity and features of proteins with structural repeats.Biophysical reviews · 2023Review
- Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein ofInternational journal of molecular sciences · 2021Article
- Identification of Amyloidogenic Regions inInternational journal of molecular sciences · 2021Article
- Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs.Frontiers in molecular biosciences · 2021Article
- Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?International journal of molecular sciences · 2020Review
- Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking.International journal of molecular sciences · 2020Article
- Macromolecular Interactions of Disordered Proteins.International journal of molecular sciences · 2020Article
- Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure.Molecules (Basel, Switzerland) · 2019Article
- The number of domains in the ribosomal protein S1 as a hallmark of the phylogenetic grouping of bacteria.PloS one · 2019Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
An important feature of ribosomal S1 proteins is multiple copies of structural domains in bacteria, the number of which changes in a strictly limited range from one to six. For S1 proteins, little is known about the contribution of flexible regions to protein domain function. We exhaustively studied a tendency for intrinsic disorder and flexibility within and between structural domains for all available UniProt S1 sequences. Using charge-hydrophobicity plot cumulative distribution function (CH-CDF) analysis we classified 53% of S1 proteins as ordered proteins; the remaining proteins were related to molten globule state. S1 proteins are characterized by an equal ratio of regions connecting the secondary structure within and between structural domains, which indicates a similar organization of separate S1 domains and multi-domain S1 proteins. According to the FoldUnfold and IsUnstruct programs, in the multi-domain proteins, relatively short flexible or disordered regions are predominant. The lowest percentage of flexibility is in the central parts of multi-domain proteins. Our results suggest that the ratio of flexibility in the separate domains is related to their roles in the activity and functionality of S1: a more stable and compact central part in the multi-domain proteins is vital for RNA interaction, terminals domains are important for other functions.
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