scholarly journals Bridging Conformational Dynamics and Function Using Single-Molecule Spectroscopy

Structure ◽  
2006 ◽  
Vol 14 (4) ◽  
pp. 633-643 ◽  
Author(s):  
Sua Myong ◽  
Benjamin C. Stevens ◽  
Taekjip Ha
Keyword(s):  
Single Molecule ◽  
Conformational Dynamics ◽  
Single Molecule Spectroscopy ◽  
Dynamics And Function ◽  
And Function

scholarly journals Single Molecule FRET Studies of Protein Conformational Landscapes: 3 Prototypic Examples for the Relation Between Conformational Dynamics and Function

2011 ◽  
Vol 100 (3) ◽  
pp. 474a-475a
Author(s):  
Markus Richert ◽  
Dymitro Rodnin ◽  
Carola S. Hengstenberg ◽  
Thomas Peulen ◽  
Alessandro Valeri ◽  
...  
Keyword(s):  
Single Molecule ◽  
Conformational Dynamics ◽  
Single Molecule Fret ◽  
Dynamics And Function ◽  
And Function

scholarly journals δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function

2016 ◽  
Vol 113 (25) ◽  
pp. 6916-6921 ◽  
Author(s):  
Eric C. Arakel ◽  
Kora P. Richter ◽  
Anne Clancy ◽  
Blanche Schwappach
Keyword(s):  
Secretory Pathway ◽  
Conformational Dynamics ◽  
Functional Complementation ◽  
Vesicle Formation ◽  
Membrane Recruitment ◽  
Early Secretory Pathway ◽  
Packing Defects ◽  
Clathrin Adaptor ◽  
Dynamics And Function ◽  
And Function

Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of δ-COP via functional complementation in yeast, we dissect the domains of the δ-COP subunit. We show that the μ-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.

scholarly journals Single-molecule biophysics: at the interface of biology, physics and chemistry

2007 ◽  
Vol 5 (18) ◽  
pp. 15-45 ◽  
Author(s):  
Ashok A Deniz ◽  
Samrat Mukhopadhyay ◽  
Edward A Lemke
Keyword(s):  
Single Molecule ◽  
Biological Molecules ◽  
Single Molecule Fluorescence ◽  
Complex Behaviour ◽  
Single Molecule Biophysics ◽  
Single Molecule Studies ◽  
Dynamics And Function ◽  
And Function ◽  
Ensemble Experiments

Single-molecule methods have matured into powerful and popular tools to probe the complex behaviour of biological molecules, due to their unique abilities to probe molecular structure, dynamics and function, unhindered by the averaging inherent in ensemble experiments. This review presents an overview of the burgeoning field of single-molecule biophysics, discussing key highlights and selected examples from its genesis to our projections for its future. Following brief introductions to a few popular single-molecule fluorescence and manipulation methods, we discuss novel insights gained from single-molecule studies in key biological areas ranging from biological folding to experiments performed in vivo .

scholarly journals Insight into helicase mechanism and function revealed through single-molecule approaches

2010 ◽  
Vol 43 (2) ◽  
pp. 185-217 ◽  
Author(s):  
Jaya G. Yodh ◽  
Michael Schlierf ◽  
Taekjip Ha
Keyword(s):  
Single Molecule ◽  
Conformational Dynamics ◽  
Magnetic Tweezers ◽  
Repetitive Behaviors ◽  
Helicase Activity ◽  
Step Size ◽  
Mechanistic Insight ◽  
Combination Of Methods ◽  
And Function ◽  
Insight Into

AbstractHelicases are a class of nucleic acid (NA) motors that catalyze NTP-dependent unwinding of NA duplexes into single strands, a reaction essential to all areas of NA metabolism. In the last decade, single-molecule (sm) technology has proven to be highly useful in revealing mechanistic insight into helicase activity that is not always detectable via ensemble assays. A combination of methods based on fluorescence, optical and magnetic tweezers, and flow-induced DNA stretching has enabled the study of helicase conformational dynamics, force generation, step size, pausing, reversal and repetitive behaviors during translocation and unwinding by helicases working alone and as part of multiprotein complexes. The contributions of these sm investigations to our understanding of helicase mechanism and function will be discussed.

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