Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization  Daniel G Flint, Janet R Kumita,

Slides:



Advertisements
Similar presentations
Volume 14, Issue 8, Pages (August 2007)
Advertisements

R.Ian Menz, John E. Walker, Andrew G.W. Leslie  Cell 
Volume 16, Issue 11, Pages (November 2009)
Crystal Structure of the Tandem Phosphatase Domains of RPTP LAR
Volume 10, Issue 5, Pages (November 2002)
The loop E–loop D region of Escherichia coli 5S rRNA: the solution structure reveals an unusual loop that may be important for binding ribosomal proteins 
Structural Basis for the Highly Selective Inhibition of MMP-13
Recombination: Pieces of the site-specific recombination puzzle
The open conformation of a Pseudomonas lipase
Volume 21, Issue 1, Pages (January 2013)
Olivier Fisette, Stéphane Gagné, Patrick Lagüe  Biophysical Journal 
Moses Prabu-Jeyabalan, Ellen Nalivaika, Celia A. Schiffer  Structure 
Crystal Structure of M. tuberculosis ABC Phosphate Transport Receptor
Volume 3, Issue 3, Pages (March 1999)
Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein Receptors  Carl Fisher, Natalia Beglova, Stephen C. Blacklow 
Β-Hairpin Folding Mechanism of a Nine-Residue Peptide Revealed from Molecular Dynamics Simulations in Explicit Water  Xiongwu Wu, Bernard R. Brooks  Biophysical.
Volume 14, Issue 3, Pages (March 2001)
Volume 124, Issue 2, Pages (January 2006)
Volume 23, Issue 1, Pages (July 2006)
Hydration and DNA Recognition by Homeodomains
Volume 108, Issue 6, Pages (March 2015)
Marina Blanco-Lomas,†,§ Subhas Samanta,‡,§ Pedro J. Campos,† G
Einav Gross, David B Kastner, Chris A Kaiser, Deborah Fass  Cell 
Michel A. Cuendet, Olivier Michielin  Biophysical Journal 
Volume 102, Issue 3, Pages (February 2012)
De Novo Design of Foldable Proteins with Smooth Folding Funnel
Crystal Structure of the MHC Class I Homolog MIC-A, a γδ T Cell Ligand
Site-specific recombination in plane view
Volume 6, Issue 10, Pages (October 1998)
Volume 21, Issue 10, Pages (October 2013)
G. Fiorin, A. Pastore, P. Carloni, M. Parrinello  Biophysical Journal 
A Molecular Dynamics Study of Ca2+-Calmodulin: Evidence of Interdomain Coupling and Structural Collapse on the Nanosecond Timescale  Craig M. Shepherd,
Volume 5, Issue 3, Pages (March 2000)
Volume 14, Issue 8, Pages (August 2007)
Volume 22, Issue 1, Pages (January 2015)
Andrew H. Huber, W.James Nelson, William I. Weis  Cell 
Volume 89, Issue 4, Pages (October 2005)
Qian Steven Xu, Rebecca B. Kucera, Richard J. Roberts, Hwai-Chen Guo 
Volume 14, Issue 5, Pages (May 2006)
Solution Structure of the Cyclotide Palicourein
Volume 95, Issue 7, Pages (December 1998)
Volume 24, Issue 8, Pages (August 2016)
Volume 95, Issue 9, Pages (November 2008)
Antonina Roll-Mecak, Chune Cao, Thomas E. Dever, Stephen K. Burley 
Structural Basis for the Highly Selective Inhibition of MMP-13
Insights into Oncogenic Mutations of Plexin-B1 Based on the Solution Structure of the Rho GTPase Binding Domain  Yufeng Tong, Prasanta K. Hota, Mehdi.
Molecular Dynamics Simulations of Wild-Type and Mutant Forms of the Mycobacterium tuberculosis MscL Channel  Donald E. Elmore, Dennis A. Dougherty  Biophysical.
Investigating Lipid Composition Effects on the Mechanosensitive Channel of Large Conductance (MscL) Using Molecular Dynamics Simulations  Donald E. Elmore,
Volume 13, Issue 7, Pages (July 2005)
Volume 6, Issue 10, Pages (October 1998)
Volume 8, Issue 4, Pages (April 2000)
Transmuting α helices and β sheets
Volume 85, Issue 5, Pages (May 1996)
Sequence Determination of Reduction Potentials by Cysteinyl Hydrogen Bonds and Peptide Dipoles in [4Fe-4S] Ferredoxins  Brian W. Beck, Qian Xie, Toshiko.
Unmasking the Annexin I Interaction from the Structure of Apo-S100A11
Amedeo Caflisch, Martin Karplus  Structure 
Volume 14, Issue 6, Pages (June 2006)
Volume 4, Issue 2, Pages (February 1996)
Crystal Structure of the Tyrosine Phosphatase SHP-2
Molecular Similarity Analysis Uncovers Heterogeneous Structure-Activity Relationships and Variable Activity Landscapes  Lisa Peltason, Jürgen Bajorath 
Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP+ molecule and provides insights into enzyme deficiency  Shannon.
The Relation between α-Helical Conformation and Amyloidogenicity
Dept. of Chemistry, University of Toronto, Canada
Structure of a HoxB1–Pbx1 Heterodimer Bound to DNA
Volume 10, Issue 4, Pages (April 2003)
Peter König, Rafael Giraldo, Lynda Chapman, Daniela Rhodes  Cell 
Mechanism of Interaction between the General Anesthetic Halothane and a Model Ion Channel Protein, III: Molecular Dynamics Simulation Incorporating a.
Characterization of Structure, Dynamics, and Detergent Interactions of the Anti-HIV Chemokine Variant 5P12-RANTES  Maciej Wiktor, Oliver Hartley, Stephan.
The Structure of Sortase B, a Cysteine Transpeptidase that Tethers Surface Protein to the Staphylococcus aureus Cell Wall  Yinong Zong, Sarkis K Mazmanian,
Hydrophobic Core Formation and Dehydration in Protein Folding Studied by Generalized-Ensemble Simulations  Takao Yoda, Yuji Sugita, Yuko Okamoto  Biophysical.
Presentation transcript:

Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization  Daniel G Flint, Janet R Kumita, Oliver S Smart, G.Andrew Woolley  Chemistry & Biology  Volume 9, Issue 3, Pages 391-397 (March 2002) DOI: 10.1016/S1074-5521(02)00109-6

Figure 1 Compatibility of Cis versus Trans Cross-Linkers with Different Cys Spacings The potential energy difference is calculated by taking the energy of the trans conformation and subtracting the energy of the cis conformation for each Cys pair spacing investigated. A positive energy difference implies that, for that Cys spacing, a peptide with a cis cross-linker will be more helical than when the linker is trans. A negative energy difference implies the opposite: that a peptide will be more helical when the linker is in the trans form than when in the cis form. Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)

Figure 2 Structures of Peptide Variants and Azobenzene Reagents A structure of the azobenzene cross-linking reagent and primary sequences of the cross-linked peptides; AZO refers to the cross-linker (1) after reaction with the two cysteine side chains. Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)

Figure 3 Energy-Optimized Molecular Models of FK-4-X Schematic models of trans FK-4-X (left) and cis FK-4-X (right). The peptide backbones are represented by a silver ribbon. The cysteine side chain and cross-linker atoms are colored according to atom type: carbon = green, nitrogen = blue, oxygen = red, and sulfur = yellow. Hydrogens are omitted for clarity. The helical model is the final frame of a 500-ps MD run after starting from a helical conformation. To generate the coil model, the peptide was built in SYBYL, and a random backbone conformation was generated. The cross-linker was then attached to the peptide, and the complete molecule was subjected to energy minimization, with the linker atoms constrained to their initial positions. A further round of energy minimization was then undertaken with all atoms free to move. Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)

Figure 4 Effects of Photoirradiation on Secondary Structure of FK-4-X (A) UV/Vis spectrum of FK-4-X (35 μM, 5 mM phosphate buffer [pH 7.0]) in the dark-adapted state (solid line) and after irradiation at 370 nm (dotted line). The spectrum of the pure cis chromophore is shown as a dash-dot line. (B) CD spectrum of FK-4-X (35 μM, 5 mM phosphate buffer [pH 7.0]) in the dark-adapted state (solid line) and after irradiation at 370 nm (dotted line). The calculated CD spectrum for the 100% cis peptide is shown as a dash-dot line. Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)

Figure 5 Energy-Optimized Molecular Models of FK-11-X Schematic models of trans FK-11 (left) and cis FK-11 (right). The peptide backbones are represented by a silver ribbon. The cysteine side chain and cross-linker atoms are colored according to atom type: carbon = green, nitrogen = blue, oxygen = red, and sulfur = yellow. Hydrogens are omitted for clarity. The helical model is the final frame of a 500-ps MD run after starting from a helical conformation. To generate the coil model, the peptide was built in SYBYL, and a random backbone conformation was generated. The cross-linker was then attached to the peptide, and the complete molecule was subjected to energy minimization, with the linker atoms constrained to their initial positions. A further round of energy minimization was then undertaken with all atoms free to move. Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)

Figure 6 Effects of Photoirradiation on Secondary Structure of FK-11-X (A) UV/Vis spectrum of FK-11-X (44 μM, 5 mM phosphate buffer [pH 7.0]) in the dark-adapted state (solid line) and after irradiation at 370 nm (dotted line). The spectrum of the pure cis chromophore is shown as a dash-dot line. (B) CD spectrum of FK-11-X (44 μM, 5 mM phosphate buffer [pH 7.0]) in the dark-adapted state (solid line) and after irradiation at 370 nm (dotted line). The calculated CD spectrum for the 100% cis peptide is shown as a dash-dot line. Inset: long-wavelength CD spectrum of FK-11-X (44 μM, 5 mM phosphate buffer [pH 7.0]) in the dark-adapted state (solid line) and after irradiation at 370 nm (dotted line). Chemistry & Biology 2002 9, 391-397DOI: (10.1016/S1074-5521(02)00109-6)