Journal Issue - Volume 19 Issue 5 (May 2010)
In This Issue
- Published in Wiley Interscience on Apr 27, 2010
- DOI: 10.1002/pro.397 (p )
A synergistic approach to protein crystallization: Combination of a fixed‐arm carrier with surface entropy reduction
- Andrea F. Moon, Geoffrey A. Mueller, Xuejun Zhong, Lars C. Pedersen
- Published in Wiley Interscience on Mar 01, 2010
- DOI: 10.1002/pro.368 (p 901-913)
Abstract Protein crystallographers are often confronted with recalcitrant proteins not readily crystallizable, or which crystallize in problematic forms. A variety of techniques have been used to surmount such obstacles: crystallization using carrier proteins or antibody complexes, chemical modification, surface entropy reduction, proteolytic digestion, and additive screening. Here we present a synergistic approach for successful...
A flexible docking scheme to explore the binding selectivity of PDZ domains
- Z. Nevin Gerek, S. Banu Ozkan
- Published in Wiley Interscience on Mar 01, 2010
- DOI: 10.1002/pro.366 (p 914-928)
Abstract Modeling of protein binding site flexibility in molecular docking is still a challenging problem due to the large conformational space that needs sampling. Here, we propose a flexible receptor docking scheme: A dihedral restrained replica exchange molecular dynamics (REMD), where we incorporate the normal modes obtained by the Elastic Network Model (ENM) as dihedral restraints to speed up the search towards correct binding...
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins
- C. Nick Pace, Beatrice M. P. Huyghues‐Despointes, Hailong Fu, Kazufumi Takano, J. Martin Scholtz, Gerald R. Grimsley
- Published in Wiley Interscience on Mar 02, 2010
- DOI: 10.1002/pro.370 (p 929-943)
Abstract The goal of this article is to gain a better understanding of the denatured state ensemble (DSE) of proteins through an experimental and computational study of their denaturation by urea. Proteins unfold to different extents in urea and the most hydrophobic proteins have the most compact DSE and contain almost as much secondary structure as folded proteins. Proteins that unfold to the greatest extent near pH 7 still contain...
Internal motion in protein crystal structures
- Andrea Schmidt, Victor S. Lamzin
- Published in Wiley Interscience on Mar 02, 2010
- DOI: 10.1002/pro.371 (p 944-953)
Abstract The binding states of the substrates and the environment have significant influence on protein motion. We present the analysis of such motion derived from anisotropic atomic displacement parameters (ADPs) in a set of atomic resolution protein structures. Local structural motion caused by ligand binding as well as functional loops showing cooperative patterns of motion could be inferred. The results are in line with proposed...
Improving the solubility of anti‐LINGO‐1 monoclonal antibody Li33 by isotype switching and targeted mutagenesis
- R. Blake Pepinsky, Laura Silvian, Steven A. Berkowitz, Graham Farrington, Alexey Lugovskoy, Lee Walus, John Eldredge, Allan Capili, Sha Mi, Christilyn Graff, Ellen Garber
- Published in Wiley Interscience on Mar 02, 2010
- DOI: 10.1002/pro.372 (p 954-966)
Abstract Monoclonal antibodies (Mabs) are a favorite drug platform of the biopharmaceutical industry. Currently, over 20 Mabs have been approved and several hundred others are in clinical trials. The anti‐LINGO‐1 Mab Li33 was selected from a large panel of antibodies by Fab phage display technology based on its extraordinary biological activity in promoting oligodendrocyte differentiation and myelination in vitro and in animal...
The terminal 5′ phosphate and proximate phosphorothioate promote ligation‐independent cloning
- Xi‐Peng Liu, Jian‐Hua Liu
- Published in Wiley Interscience on Mar 09, 2010
- DOI: 10.1002/pro.374 (p 967-973)
Abstract Function studies of many proteins are waited to develop after genome sequencing. High‐throughout technology of gene cloning will strongly promote proteins' function studies. Here we describe a ligation‐independent cloning (LIC) method, which is based on the amplification of target gene and linear vector by PCR using phosphorothioate‐modified primers and the digestion of PCR products by λ exonuclease. The phosphorothioate...
Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C‐terminal domain phosphatase, Scp1
- Mengmeng Zhang, June Liu, Youngjun Kim, Jack E. Dixon, Samuel L. Pfaff, Gordon N. Gill, Joseph P. Noel, Yan Zhang
- Published in Wiley Interscience on Mar 10, 2010
- DOI: 10.1002/pro.375 (p 974-986)
Abstract Human small C‐terminal domain phosphatase 1 (Scp1) modulates the phosphorylation state of the C‐terminal domain (CTD) of eukaryotic RNA polymerase II (RNAP II), with preference for phosphorylated Ser5 in the tandem heptad repeats of the CTD. Additionally, Scp1 was identified as a conserved regulator of neuronal stem cell development. Scp1 is a member of haloacid dehalogenase (HAD) superfamily, whose catalysis depends on a...
Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity
- Javier García‐Nafría, Gabriela Ondrovičová, Elena Blagova, Vladimir M. Levdikov, Jacob A. Bauer, Carolyn K. Suzuki, Eva Kutejová, Anthony J. Wilkinson, Keith S. Wilson
- Published in Wiley Interscience on Mar 10, 2010
- DOI: 10.1002/pro.376 (p 987-999)
Abstract ATP‐dependent proteases are crucial for cellular homeostasis. By degrading short‐lived regulatory proteins, they play an important role in the control of many cellular pathways and, through the degradation of abnormally misfolded proteins, protect the cell from a buildup of aggregates. Disruption or disregulation of mammalian mitochondrial Lon protease leads to severe changes in the cell, linked with carcinogenesis,...
Design, selection, and characterization of a split chorismate mutase
- Manuel M. Müller, Hajo Kries, Eva Csuhai, Peter Kast, Donald Hilvert
- Published in Wiley Interscience on Mar 19, 2010
- DOI: 10.1002/pro.377 (p 1000-1010)
Abstract Split proteins are versatile tools for detecting protein–protein interactions and studying protein folding. Here, we report a new, particularly small split enzyme, engineered from a thermostable chorismate mutase (CM). Upon dissecting the helical‐bundle CM from Methanococcus jannaschii into a short N‐terminal helix and a 3‐helix segment and attaching an antiparallel leucine zipper dimerization domain to the individual...
Backbone additivity in the transfer model of protein solvation
- Char Y. Hu, Hironori Kokubo, Gillian C. Lynch, D. Wayne Bolen, B. Montgomery Pettitt
- Published in Wiley Interscience on Mar 19, 2010
- DOI: 10.1002/pro.378 (p 1011-1022)
Abstract The transfer model implying additivity of the peptide backbone free energy of transfer is computationally tested. Molecular dynamics simulations are used to determine the extent of change in transfer free energy (ΔGtr) with increase in chain length of oligoglycine with capped end groups. Solvation free energies of oligoglycine models of varying lengths in pure water and in the osmolyte solutions, 2M urea and 2M trimethylamine N‐oxide...
Dimer–monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transfer
- Filippo Genovese, Stefania Ferrari, Giambattista Guaitoli, Monica Caselli, M. Paola Costi, Glauco Ponterini
- Published in Wiley Interscience on Mar 19, 2010
- DOI: 10.1002/pro.379 (p 1023-1030)
Abstract An ad hoc bioconjugation/fluorescence resonance energy transfer (FRET) assay has been designed to spectroscopically monitor the quaternary state of human thymidylate synthase dimeric protein. The approach enables the chemoselective engineering of allosteric residues while preserving the native protein functions through reversible masking of residues within the catalytic site, and is therefore suitable for...
Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
- Arthur Laganowsky, Justin L. P. Benesch, Meytal Landau, Linlin Ding, Michael R. Sawaya, Duilio Cascio, Qingling Huang, Carol V. Robinson, Joseph Horwitz, David Eisenberg
- Published in Wiley Interscience on Mar 29, 2010
- DOI: 10.1002/pro.380 (p 1031-1043)
Abstract Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystallin (AAC59–163) and human alphaB crystallin (ABC68–162), both containing the C‐terminal extension that functions in chaperone action and oligomeric assembly. In both structures, ...
Increasing protein stability: Importance of Δ C p and the denatured state
- Hailong Fu, Gerald Grimsley, J. Martin Scholtz, C. Nick Pace
- Published in Wiley Interscience on Mar 25, 2010
- DOI: 10.1002/pro.381 (p 1044-1052)
Abstract Increasing the conformational stability of proteins is an important goal for both basic research and industrial applications. In vitro selection has been used successfully to increase protein stability, but more often site‐directed mutagenesis is used to optimize the various forces that contribute to protein stability. In previous studies, we showed that improving electrostatic interactions on the protein surface and...
Interruptions in the collagen repeating tripeptide pattern can promote supramolecular association
- Eileen S. Hwang, Geetha Thiagarajan, Avanish S. Parmar, Barbara Brodsky
- Published in Wiley Interscience on Mar 25, 2010
- DOI: 10.1002/pro.383 (p 1053-1064)
Abstract The standard collagen triple‐helix requires a perfect (Gly‐Xaa‐Yaa)n sequence, yet all nonfibrillar collagens contain interruptions in this tripeptide repeating pattern. Defining the structural consequences of disruptions in the sequence pattern may shed light on the biological role of sequence interruptions, which have been suggested to play a role in molecular flexibility, collagen degradation, and ligand binding. Previous studies...




