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Conformational Transitions

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Protein Structure and Modeling

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Abstract

Protein molecules are dynamic bodies. They form and disassemble complexes, channel substrates, and rotate, changing conformational states to perform their functions. Small motions in the enzyme active site, large rearrangements of subunits and sliding along the filaments involve conformations changes.

Conformational transitions occur in many forms: change in orientation of hemoglobin subunits in oxygenated/deoxygenated states, proteolytic cleavage and conversion of precursors to mature molecules of fibrin/fibrinogen , helix coil transitions or changes between left handed and right handed orientation of helices.

The transitions of the molecule or molecular assembly largely depend on conformational changes of the constituent parts, amino acids. Rotameric states of the backbone and side chains change and these changes add up and propagate to provide large scale motions of the molecular parts. Micro motions and macro motions provide basis for conformational transitions.

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Authors and Affiliations

  1. Department of Biophysics, School of Theoretical Modeling, Washington, DC, USA

    Natalya Kurochkina

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  1. Natalya Kurochkina
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Kurochkina, N. (2019). Conformational Transitions. In: Protein Structure and Modeling. Springer, Singapore. https://doi.org/10.1007/978-981-13-6601-7_2

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