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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Enzymes and Activation Energy01:13

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The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...
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Activating an enzyme by an engineered coiled coil switch.

Satoshi Yuzawa1, Toshihisa Mizuno, Toshiki Tanaka

  • 1Graduate School of Material Science, Nagoya Institute of Technology, Gokiso-cho, Nagoya 466-8555, Japan.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|July 26, 2006
PubMed
Summary
This summary is machine-generated.

Scientists engineered a circular protein variant of RNase T1 (Ribonuclease T1) to control its enzymatic activity using peptide binding. This novel protein design restores enzyme function through specific peptide interactions.

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Area of Science:

  • Protein engineering
  • Biochemistry
  • Molecular biology

Background:

  • Circularly permuted proteins offer unique structural and functional properties.
  • Engineered peptide binding sites can modulate protein activity.
  • Ribonuclease T1 (RNaseT1) is a well-characterized enzyme whose activity can be studied through structural modifications.

Purpose of the Study:

  • To design a de novo protein with tunable enzymatic activity.
  • To investigate the refolding and restoration of enzymatic activity in a circularly permuted RNaseT1 mutant.
  • To utilize engineered peptide interactions for protein function control.

Main Methods:

  • Circular permutation of RNaseT1 by tethering termini and introducing a cleavage site.
  • Construction and application of ABC-type heterotrimeric coiled coil peptides.
  • Fusion of coiled coil peptides to the N- and C-termini of the circular RNaseT1 mutant.
  • Assay of enzymatic activity restoration upon peptide addition.

Main Results:

  • A circular permutant of RNaseT1 was created, initially lacking enzymatic activity due to structural destabilization.
  • Fusion of specific coiled coil peptides (A and B) to the permuted RNaseT1.
  • Addition of a complementary coiled coil peptide (C) induced refolding and restored RNaseT1 enzymatic activity.
  • The refolding mechanism relies on the coiled coil structure bringing cleaved sites into proximity.

Conclusions:

  • Enzymatic activity of RNaseT1 can be reversibly controlled through engineered peptide binding to a circularly permuted variant.
  • This study demonstrates a novel strategy for de novo protein design and functional modulation.
  • The findings have implications for developing switchable enzymes and protein-based molecular devices.