Subject: | Protein Folding |
Presenter: | Alena Shmygelska |
Paper: | " Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics " |
  | by KW Plaxco, KT Simons, I Ruczinski, and D Baker |
Abstract |
Topology, Stability, Sequence, and Length
The folding rate of single domain proteins following two state kinetics
can differ up to millions of times in magnitude. Plaxco et al. in their
paper "Topology, Stability, Sequence, and Length: Defining the
Determinants of Two-State Protein Folding Kinetics" summarized their
experiments and findings on which of the factors cause such a
spread in folding speeds. They found that folding process is not very
sensitive to the finest details of the sequence, but rather it depends on
the large-scale topological properties of the sequence.
Reference:
KW Plaxco, KT Simons, I Ruczinski, and D Baker. (2000). Topology, Stability,
Sequence, and Length: Defining the Determinants of Two-State Protein Folding
Kinetics. Biochemistry. Sept 19; 39(37):11177-83.
The paper is available at http://www.cs.ubc.ca/labs/beta/Courses/BioinfoReadingGroup/Winter2003/plaxco.pdf
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