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Mosberg Lab - University of Michigan

The Mosberg Lab studies peptide synthesis and molecular recognition at the University of Michigan in Ann Arbor.

http://mosberglab.phar.umich.edu/

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Mosberg Lab - University of Michigan | mosberglab.phar.umich.edu Reviews

https://mosberglab.phar.umich.edu

The Mosberg Lab studies peptide synthesis and molecular recognition at the University of Michigan in Ann Arbor.

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mosberglab.phar.umich.edu mosberglab.phar.umich.edu
1

Mosberg Lab - Publications

http://mosberglab.phar.umich.edu/publications

Antonenko Y.N., Gluhov G.S., Firsov am, Pogozheva I.D., Kovalchuk S.I., Pechnikova E.V., Kotova E.A., Sokolova O.S. Gramicidin A disassembles large conductive clusters of its lysine-substituted derivatives in lipid membranes. Phys Chem Chem Phys. Geng J., Pogozheva I.D., Mosberg H.I., Raghavan M. Use of functional polymorphisms to elucidate the peptide binding site of TAP complexes. Bender am, Clark M.J., Agius M.P., Traynor J.R., Mosberg H.I. Bioorg Med Chem Lett. Life at the border: adaptation of prote...

2

Mosberg Lab - Resources

http://mosberglab.phar.umich.edu/resources

GnRHR HUMAN AD GnRH. Human gonadotropin-releasing hormone receptor (active state, residues 11-328) with GnRH (residues 1-10) and C-terminus of Gq (residues 330-359). GnRHR HUMAN ID cetrorelix. Human gonadotropin-releasing hormone receptor (inactive state, residues 11-328) with cetrorelix (residues 1-10). MC1R HUMAN ID ASIP. MC1 melanocortin receptor (inactive state, residues 35-317) with ASIP (residues 93-132). MC2R HUMAN AD ACTH. ACTH receptor (active state, residues 12-295) with ACTH (residues 1-24).

3

Mosberg Lab - About Us

http://mosberglab.phar.umich.edu/aboutUs.php

About Us - Projects. Research in our lab focuses primarily on molecular recognition between small to medium size ligands (usually peptides) and their macromolecular targets (usually membrane-associated, G protein-coupled receptors, GPCRs) and spans structure-based drug design and synthesis, combinatorial synthesis, protein structure modeling, and biochemical characterization. 1 Development of mixed efficacy opioid ligands. 2 Design and synthesis of biologically active opioid peptides and peptidomimetics.

4

Mosberg Lab - People

http://mosberglab.phar.umich.edu/people

Henry I. Mosberg. Aubrie A. Harland. Aaron M. Bender. Anthony F. Nastase. Sean P. Henry. Front row, left-to-right: Andrei, HIM, Beth, Mary, Kate. Back row, left-to-right: Irina, Jess, Lauren, Jon Pollock (REU student 2010). Carol B. Fowler. Lauren C. Purington. Elizabeth A. Girnys. Vanessa R. Porter.

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opm.phar.umich.edu opm.phar.umich.edu

Species - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/species.php

PDB ID or protein name. All proteins in OPM. Acanthoscurria gomesiana (Tarantula spider). Actinia fragacea (Strawberry anemone). Aedes aegypti (Yellowfever mosquito). Ambystoma tigrinum (Tiger salamander). Amycolatopsis orientalis (Nocardia orientalis). Androctonus australis (Sahara scorpion). Androctonus mauretanicus mauretanicus (Scorpion). Anguilla japonica (Japanese eel). Anopheles gambiae (African malaria mosquito). Anthopleura elegantissima (Sea anemone). Avian infectious bursal disease virus.

opm.phar.umich.edu opm.phar.umich.edu

Proteins - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/proteins.php

PDB ID or protein name. All proteins in OPM. All proteins in OPM (3142 proteins). Num TM Sec. Structs. Hydrophobic Thickness or Depth (Å). Tilt Angle (°). Sensory rhodopsin, monomer. 319 ± 1.5. 13 ± 4. 318 ± 1.1. 0 ± 1. Sensory rhodopsin II, tetramer. 305 ± 1.1. 0 ± 0. 318 ± 1.4. 0 ± 1. 318 ± 1.3. 9 ± 2. Bacteriorhodopsin, K state, with lipids. 300 ± 0.6. 0 ± 0. Bacteriorhodopsin, trimer, complex with annular lipids. 298 ± 0.6. 0 ± 0. Sensory rhodopsin II, monomer. 303 ± 1.5. 15 ± 2. 296 ± 2.2. Squid rho...

opm.phar.umich.edu opm.phar.umich.edu

Families - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/families.php

PDB ID or protein name. All proteins in OPM. Microbial and algal rhodopsins. 35 proteins) 3.E.1 (TCDB). G-protein coupled receptors, family A. 74 proteins) 9.A.14 (TCDB). GPCR Secretin (B) family. 4 proteins) 9.A.14 (TCDB). 6 proteins) 9.A.14 (TCDB). GPCR Metabotropic glutamate receptor (C) family. 2 proteins) 9.A.14 (TCDB). 1 protein) 1.C.113 (TCDB). Photosynthetic reaction centers from bacteria. 5 proteins) 3.E.2 (TCDB). 6 proteins) 5.B.4 (TCDB). 6 proteins) 5.B.4 (TCDB). 1 protein) 5.A.3 (TCDB). Trans...

opm.phar.umich.edu opm.phar.umich.edu

Classification - About OPM - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/about.php?subject=classification

PDB ID or protein name. All proteins in OPM. Comparision with experimental data. Comparision with other computational methods. OPM consists of quaternary complexes (biological units) that are classified based on the structure of their main transmembrane or membrane-associated domain. The classification was built using SCOP. But it differs from both systems in certain aspects. There are four levels of hierarchy in the classification:. Evolutionarily related proteins with superimposable 3D structures.

opm.phar.umich.edu opm.phar.umich.edu

Localization (target membrane) - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/localization.php

PDB ID or protein name. All proteins in OPM. Bacterial Gram-negative inner membrane. Bacterial Gram-negative outer membrane. Bacterial Gram-positive outer membrane. Bacterial Gram-positive plasma membrane. University of Michigan, Ann Arbor, MI 48109 USA.

opm.phar.umich.edu opm.phar.umich.edu

Methods - About OPM - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/about.php?subject=methods

PDB ID or protein name. All proteins in OPM. Comparision with experimental data. Comparision with other computational methods. Each protein is considered as rigid body that freely floats in a hydrophobic slab of adjustable thickness. Orientation of the protein was determined by minimizing its transfer energy, ΔG. With respect to d. Variables in a coordinate system whose axis Z coincides with the bilayer normal:. Schematic representation of a transmembrane protein in a hydrophobic slab. Profiles of hydrog...

opm.phar.umich.edu opm.phar.umich.edu

Comparision with experimental data - About OPM - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/about.php?subject=experiments

PDB ID or protein name. All proteins in OPM. Comparision with experimental data. Comparision with other computational methods. Comparison with experimental data. Comparison of computational results for transmembrane proteins with experimental studies of protein orientations in membranes. XSC, SL, CL, EM. Blaurock and Wilkins 1972; Barclay and Findlay 1984, Davison and Findlay 1986a,b; Hubbell et al. 2003, Krebs et al. 2003. SL, NMR, HM. Wegener et al. 2000. Photoreaction center from Rh. Spaeroides. Voss ...

opm.phar.umich.edu opm.phar.umich.edu

Membrane Protein Lipid Composition Atlas - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/atlas.php

PDB ID or protein name. All proteins in OPM. Membrane Protein Lipid Composition Atlas. Bacterial Gram-negative inner membrane. Bacterial Gram-negative outer membrane. Bacterial Gram-positive outer membrane. Bacterial Gram-positive plasma membrane. Nat Rev Mol Cell Biol. 2008 Feb;9(2):112-24. Membrane lipids: where they are and how they behave. University of Michigan, Ann Arbor, MI 48109 USA.

opm.phar.umich.edu opm.phar.umich.edu

PPM Server - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/server.php

PDB ID or protein name. All proteins in OPM. University of Michigan, Ann Arbor, MI 48109 USA.

opm.phar.umich.edu opm.phar.umich.edu

Features - About OPM - Orientations of Proteins in Membranes (OPM) database

http://opm.phar.umich.edu/about.php?subject=features

PDB ID or protein name. All proteins in OPM. Comparision with experimental data. Comparision with other computational methods. Of the proteins with calculated membrane boundaries are available for downloading separately for each protein or for a whole dataset. The coordinate files differ from original PDB entries:. The original PDB coordinates are transformed so that the calculated membrane normal coincides with the Z axis, the origin of coordinates corresponds to the middle of membrane.

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