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Review
. 2017 Feb:42:1-5.
doi: 10.1016/j.sbi.2016.10.001. Epub 2016 Oct 15.

Visualizing the nanoscale: protein internal dynamics and neutron spin echo spectroscopy

David Je Callaway  1 , Zimei Bu  2
Affiliations
Review

Visualizing the nanoscale: protein internal dynamics and neutron spin echo spectroscopy

David Je Callaway et al. Curr Opin Struct Biol. 2017 Feb.

Abstract

The most complex molecular machines are proteins found within cells. Protein dynamics, in particular dynamics on nanoscales, presents us with a novel paradigm for cell signaling: the idea that proteins and protein complexes can communicate directly within themselves to effect long-range information transfer, via coupled domains and correlated residue clusters. This idea has been little explored, in large part because of a paucity of experimental techniques that can address the necessary questions. Here we review recent progress in developing a promising new approach, neutron spin echo spectroscopy.

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Figures

Figure 1
Figure 1. NHERF1 alone can be described by a rigid-body model
Comparing experimental Deff(Q) of NHERF1 (black open squares) with rigid-body calculation (black solid line).
Figure 2
Figure 2. Selective deuteration highlights the activation of domain motion in NHERF1 upon binding to Ezrin FERM domain
(A) Comparing NSE data with rigid model calculations for the NHERF1·dFERM and NHERF1·hFERM complexes using the coordinates of the docked domains. (B) Comparing experimental Deff(Q) with calculations incorporating interdomain motion (via the mobility tensor) between PDZ1 and PDZ2, for NHERF1·dFERM (dashed red line) and NHERF1·hFERM (dashed blue line).
See this image and copyright information in PMC

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References

    1. Howard J. Mechanics of Motor Proteins and the Cytoskeleton. Sinauer Associates; Sunderland, MA: 2001. Large macromolecular machines utilize overdamped motions. See chapter 3, especially Table 3.4 on page 39.
    1. Doi M, Edwards SF. The theory of polymer dynamics. Oxford University Press; Oxford; 1986. pp, Excellent introduction to nonequilibrium statistical mechanics of macromolecular dynamics.
    1. Wax N. In: (1954) Noise and stochastic processes. Wax Nelson., editor. Vol. 1. New York: Dover Publication; 1954. Classic text on Brownian motion.
    1. Dziubinski M, Daniluk P, Lesyng B. ResiCon: a method for the identification of dynamic domains, hinges and interfacial regions in proteins. Bioinformatics. 2016;32:25–34. - PubMed
    1. Bu Z, Biehl R, Monkenbusch M, Richter D, Callaway DJ. Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy. Proc Natl Acad Sci U S A. 2005;102:17646–17651. Introduces the mobility tensor into NSE analysis. The mobility tensor determines the dynamical coupling between protein domains. Taq polymerase utilizes correlated domain dynamics over 70 Å to coordinate nucleotide synthesis and cleavage during DNA synthesis and repair. - PMC - PubMed

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