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Conformational change information


Conformational changes can elicit the motion of a protein complex. Kinesin walking on a microtubule is a molecular biological machine using protein domain dynamics on nanoscales

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.

A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a conformational change. Factors that may induce such changes include temperature, pH, voltage, light in chromophores, concentration of ions, phosphorylation, or the binding of a ligand. Transitions between these states occur on a variety of length scales (tenths of Å to nm) and time scales (ns to s), and have been linked to functionally relevant phenomena such as allosteric signaling[1] and enzyme catalysis.[2]

  1. ^ Bu Z, Callaway DJ (2011). "Proteins move! Protein dynamics and long-range allostery in cell signaling". Protein Structure and Diseases. Vol. 83. pp. 163–221. doi:10.1016/B978-0-12-381262-9.00005-7. ISBN 9780123812629. PMID 21570668. {{cite book}}: |journal= ignored (help)
  2. ^ Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T (December 2009). "Hidden alternative structures of proline isomerase essential for catalysis". Nature. 462 (7273): 669–73. Bibcode:2009Natur.462..669F. doi:10.1038/nature08615. PMC 2805857. PMID 19956261.

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Conformational change

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In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually...

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Conformation

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between the biological activity and the conformation or conformational changes of a biomolecule Equine conformation evaluates the degree of correctness of...

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Serpin

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spontaneous conformational change of this serpin to the latent conformation. Certain non-inhibitory serpins also use the serpin conformational change as part...

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Coronavirus spike protein

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proteins, the spike protein in its pre-fusion conformation is in a metastable state. A dramatic conformational change is triggered to induce the heptad repeats...

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Allosteric regulation

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that a conformational change in one induces a similar change in the others. Thus, all enzyme subunits do not necessitate the same conformation. Moreover...

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Agonist

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induces a conformational change and activates the receptor. This conformational change is often the result of small changes in charge or changes in protein...

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Protein structure

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structure. Conformational ensembles have been devised as a way to provide a more accurate and 'dynamic' representation of the conformational state of intrinsically...

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ATP synthase

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developed the binding change, or flip-flop, mechanism theory, which postulated that ATP synthesis is dependent on a conformational change in ATP synthase generated...

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Chromophore

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detect light energy, the chromophore is the moiety that causes a conformational change in the molecule when hit by light. Just like how two adjacent p-orbitals...

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Allosteric enzyme

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enzymes that change their conformational ensemble upon binding of an effector (allosteric modulator) which results in an apparent change in binding affinity...

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Visual phototransduction

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isomerisation, changing from the 11-cis-retinal to the all-trans-retinal configuration. Opsin therefore undergoes a conformational change to metarhodopsin...

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Reuptake

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structure of LeuT in the inward-open conformation subsequently demonstrated that the major component of the conformational change represents movement of the bundle...

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Testin

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interact with each other. Garvalov et al. propose that TES exists in two conformational states: A 'closed' state where the N & C halves of TES interact, obscuring...

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Biostasis

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molecular chaperones facilitate changes in shape (conformational change) of macromolecules in response to changes in environmental factors like temperature...

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Allosteric modulator

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conformational changes associated with the agonist-bound state. This increases the probability that the receptor will be in the active conformation,...

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Sequential model

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subunits of multimeric proteins have two conformational states. The binding of the ligand causes conformational change in the other subunits of the multimeric...

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TetR

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regulatory domain. When tetracycline binds this cavity, it causes a conformational change that affects the DNA-binding domain so that TetR is no longer able...

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Protein tertiary structure

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are held in a high-energy conformation. When the local pH drops, the protein undergoes an energetically favorable conformational rearrangement that enables...

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ABC transporter

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exporters is greater in the inward-facing conformation. A model that describes the conformational changes in the nucleotide-binding domain (NBD) as a...

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Antithrombin

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be modelled due to its conformational flexibility, and amino acids P9-P14 are not seen in this structure. This conformational flexibility indicates an...

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Cell signaling

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signal either by binding to a specific chemical or by undergoing a conformational change when interacting with physical agents. It is the specificity of...

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Protein

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are usually referred to as "conformations", and transitions between them are called conformational changes. Such changes are often induced by the binding...

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Hemoglobin

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remaining three monomers in the tetramer, where it induces a similar conformational change in the other heme sites such that binding of oxygen to these sites...

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Plasmin

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an intermediate plasminogen structure suggests that plasminogen conformational change to the open form is initiated through KR-5 transiently peeling away...

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