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Detailed characterization of the earliest events in protein folding

  • Author(s): Rosen, Laura
  • Advisor(s): Marqusee, Susan
  • et al.
Abstract

A major goal in biology is to understand how the amino acid sequence encodes all aspects of a protein's structure and dynamics. A protein spends most of its time in its fully folded native state but it also transiently populates high-energy, partially folded states. These high-energy states can be important for function and regulation, in addition to their importance to protein folding (the process by which a protein folds to its native state from the fully unfolded state). Together, all of these conformational states and the dynamics within and between them constitute a protein's energy landscape. Only by fully characterizing protein energy landscapes of model systems can we make progress on understanding all of the information encoded in an amino acid sequence. The present work makes a significant contribution to this effort by providing a detailed characterization of the high-energy, partially folded states that are most difficult to access - those populated earliest in protein folding - for an important protein folding model system, ribonuclease H (RNase H).

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