2019年5月22日水曜日

[statphys:05678] Seminar (Folding Pathway Heterogeneity in Proteins)

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Speaker: Prof. Athi N. Naganathan,
  Indian Institute of Technology Madras (IITM)
http://pbl.biotech.iitm.ac.in/athi-n.-naganathan.html

Title: Folding Pathway Heterogeneity in Proteins

Time: 13:00-14:00, 29th May

Room: Lecture room 341 (3rd build. of School of Engineering, Nagoya
University)
http://www.nagoya-u.ac.jp/access-map/index.html
http://en.nagoya-u.ac.jp/map/index.html

Abstract:
How many structurally different microscopic routes are accessible to a
protein molecule while folding? We answer this fundamental question by
analyzing 100,000 folding events generated from the
Wako-Saitô-Muñoz-Eaton statistical mechanical model incorporating
detailed energetics from more than a million conformational states on
five single-domain proteins. We find that a minimum of ~3−200
microscopic routes, with a diverse ensemble of transition-path
structures, are required to account for the total folding flux. The
partitioning of flux amongst the numerous pathways is observed to be
subtly dependent on the experimental conditions that modulate protein
stability, topological complexity and the structural resolution at which
the folding events are observed. Phi-values, experimentally measurable
features of transition state ensembles, are shown to be heterogenous at
the single-molecule level with only the average observed in ensemble
protein-engineering studies.