Sequence and structural analysis of cellular retinoic acid‐binding proteins reveals a network of conserved hydrophobic interactions
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Summary
The results presented here correlate well with available experimental evidence on folding of CRABPs and their family members and suggest future experiments, and shows the usefulness of considering pair‐wise conservation based on a simple classification of amino acids, in analyzing sequences and structures to find common core regions among homologues.
- Type
- article
- Published
- 2003-09-04
- Cited by
- 43
- References
- 72
- OpenAlex
- https://openalex.org/W1974138195
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:11850451
Keywords
Conserved sequence, Amino acid, Biology, Folding (DSP implementation), Protein Data Bank (RCSB PDB)
References
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- A possible role for π‐stacking in the self‐assembly of amyloid fibrils
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- Crystal structures of holo and apo-cellular retinol-binding protein II.
Cited by
- Functional Drift of Sequence Attributes in the FK506-Binding Proteins (FKBPs)
- Characterization of the early interactions on the folding pathway of the ileal lipid -binding protein by 19F-NMR
- In Vivo Labeling Of A Model β-Clam Protein With A Fluorescent Amino Acid
- Chapter 3: A fluorescent window into protein folding and aggregation in cells.
- Components of a Protein Machine: Allosteric Domain Assembly and a Disordered C-terminus Enable the Chaperone Functions of Hsp70
- Accurate and robust mechanical modeling of proteins
- Analysis of conservation in the Fas-associated death domain protein and the importance of conserved tryptophans in structure, stability and folding.
- Evolutionary coupling of structural and functional sequence information in the intracellular lipid‐binding protein family
- Extended Polyglutamine Tracts Cause Aggregation and Structural Perturbation of an Adjacent β Barrel Protein*
- Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology
- Roles of beta-turns in protein folding: from peptide models to protein engineering.
- "Hot cores" in proteins: Comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms
- Determinants of protein stability and folding: Comparative analysis of beta‐lactoglobulins and liver basic fatty acid binding protein
- Long-Range Effects of a Peripheral Mutation on the Enzymatic Activity of Cytochrome P450 1A2
- Recognition of Functional Sites in Protein Structures
- Tuning the Electronic Absorption of Protein-Embedded all-trans-Retinal
- Energy landscapes of functional proteins are inherently risky
- Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold‐type I, pyridoxal‐5′‐phosphate‐dependent enzymes
- A delicate balance between functionally required flexibility and aggregation risk in a β-rich protein
- The role of aromatic-aromatic interactions in strand-strand stabilization of β-sheets
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