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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Correlation between posttranslational modification and intrinsic disorder in protein.

Jianjiong Gao1, Dong Xu

  • 1Department of Computer Science, CS Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, USA.

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
|December 17, 2011
PubMed
Summary

Protein intrinsic disorder influences many post-translational modifications (PTMs). Many PTMs occur in disordered regions, while some favor ordered regions, impacting protein function and structure.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Protein intrinsic disorder plays a role in post-translational modifications (PTMs).
  • Understanding the relationship between protein disorder and PTMs is crucial for deciphering protein function.
  • UniProt/Swiss-Prot and Protein Data Bank (PDB) are key resources for studying protein structure and modifications.

Purpose of the Study:

  • To systematically investigate the correlation between protein disorder and various post-translational modifications (PTMs).
  • To identify PTMs that preferentially occur in disordered or ordered protein regions.
  • To explore how PTMs might induce disorder-to-order transitions.

Main Methods:

  • Analysis of protein disorder across numerous PTMs using UniProt/Swiss-Prot data.
  • Examination of 3-D protein structures solved by Nuclear Magnetic Resonance (NMR) from the Protein Data Bank (PDB).
  • Statistical analysis to determine preferences of PTMs for disordered versus ordered regions.

Main Results:

  • Many PTMs, including phosphorylation, hydroxylation, and methylation, show a preference for disordered regions.
  • Several PTMs, such as 4-aspartylphosphate and FMN conjugation, prefer ordered regions.
  • Acetyllysine showed no significant preference for either region.
  • NMR structure analysis indicated that certain PTMs can induce disorder-to-order transitions.

Conclusions:

  • Protein disorder is a significant factor influencing the location and potentially the function of many PTMs.
  • The study provides insights into the diverse roles of protein disorder in PTMs.
  • Disorder-to-order transitions induced by PTMs highlight the dynamic nature of protein structure and function.