Focus on protein dynamics
In this issue - pv
doi:10.1038/nchembio.254
Table of contents
November 2009, Volume 5 No 11 pp773-862
About the coverFocus on Protein Dynamics
- Focus issue:
- Novust 2009 Volume 5, No 11
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Editorial
Focus on protein dynamics
Eyes wide open - p773
doi:10.1038/nchembio.258
Understanding how proteins function in isolation and in their native context requires a merging of molecular-level techniques that explore the interplay of protein structure and dynamics.
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Commentaries
Focus on protein dynamics
Post-reductionist protein science, or putting Humpty Dumpty back together again - pp774 - 777
Lila M Gierasch & Anne Gershenson
doi:10.1038/nchembio.241
In their native environments, proteins perform their biological roles in highly concentrated viscous solutions and in complex networks with numerous partners. Yet for many years, the normal practice has been to purify a protein of interest in order to characterize its structural and functional properties. In this Commentary, we discuss how protein scientists are now tackling the theoretical and methodological challenges of studying proteins in their physiological context.
Full Text - Post-reductionist protein science, or putting Humpty Dumpty back together again | PDF (1,174 KB) - Post-reductionist protein science, or putting Humpty Dumpty back together again
Focus on protein dynamics
The nanny model for IDPs - pp778 - 781
Peter Tsvetkov, Nina Reuven & Yosef Shaul
doi:10.1038/nchembio.233
Intrinsically disordered proteins (IDPs) are subject to ubiquitin-independent degradation, a default and passive process. We describe here a model wherein a group of 'nanny' proteins function to protect newly synthesized IDPs from degradation by default, thereby insuring their maturation into important regulatory molecules.
Full Text - The nanny model for IDPs | PDF (740 KB) - The nanny model for IDPs
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News and Views
Locking out viral replication - pp782 - 783
Darren W Begley & Gabriele Varani
doi:10.1038/nchembio.245
Few antimicrobial drugs function by directly targeting RNA. A small molecule that binds the hepatitis C viral genome by 'locking' in a particular RNA conformation to inhibit viral protein production suggests a new paradigm for drug design.
Full Text - Locking out viral replication | PDF (685 KB) - Locking out viral replication
The physical chemistry of membrane curvature - pp783 - 784
Jay T Groves
doi:10.1038/nchembio.247
Membrane curvature sensing by amphipathic helices is an emergent property of the ensemble of molecules and membrane sites. New data suggest that individual molecules do not experience stronger binding to curved membranes.
Full Text - The physical chemistry of membrane curvature | PDF (234 KB) - The physical chemistry of membrane curvature
Slow growth leads to a switch - pp784 - 785
Keith Shearwin
doi:10.1038/nchembio.248
Synthetic biologists aim to rationally design and construct useful biological circuits. However, perturbation of host cell physiology, through the very process of turning on an artificial circuit, can give rise to unexpected emergent behaviors, such as bistability.
Full Text - Slow growth leads to a switch | PDF (492 KB) - Slow growth leads to a switch
Research highlights - pp786 - 787
doi:10.1038/nchembio.253
Full Text - Research highlights | PDF (204 KB) - Research highlights
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Perspective
Focus on protein dynamics
The role of dynamic conformational ensembles in biomolecular recognition - pp789 - 796
David D Boehr, Ruth Nussinov & Peter E Wright
doi:10.1038/nchembio.232
Abstract - The role of dynamic conformational ensembles in biomolecular recognition | Full Text - The role of dynamic conformational ensembles in biomolecular recognition | PDF (573 KB) - The role of dynamic conformational ensembles in biomolecular recognition
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Reviews
Focus on protein dynamics
Computer-aided design of functional protein interactions - pp797 - 807
Daniel J Mandell & Tanja Kortemme
doi:10.1038/nchembio.251
Abstract - Computer-aided design of functional protein interactions | Full Text - Computer-aided design of functional protein interactions | PDF (898 KB) - Computer-aided design of functional protein interactions
Focus on protein dynamics
NMR spectroscopy brings invisible protein states into focus - pp808 - 814
Andrew J Baldwin & Lewis E Kay
doi:10.1038/nchembio.238
Abstract - NMR spectroscopy brings invisible protein states into focus | Full Text - NMR spectroscopy brings invisible protein states into focus | PDF (936 KB) - NMR spectroscopy brings invisible protein states into focus
Focus on protein dynamics
Targeting proteins for degradation - pp815 - 822
Erin K Schrader, Kristine G Harstad & Andreas Matouschek
doi:10.1038/nchembio.250
Abstract - Targeting proteins for degradation | Full Text - Targeting proteins for degradation | PDF (1,048 KB) - Targeting proteins for degradation
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Brief Communication
Conformational inhibition of the hepatitis C virus internal ribosome entry site RNA - pp823 - 825
Jerod Parsons, M Paola Castaldi, Sanjay Dutta, Sergey M Dibrov, David L Wyles & Thomas Hermann
doi:10.1038/nchembio.217
Abstract - Conformational inhibition of the hepatitis C virus internal ribosome entry site RNA | Full Text - Conformational inhibition of the hepatitis C virus internal ribosome entry site RNA | PDF (318 KB) - Conformational inhibition of the hepatitis C virus internal ribosome entry site RNA | Supplementary information | Chemical compounds
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Top of pageArticles
Mechanism-based tuning of a LOV domain photoreceptor - pp827 - 834
Brian D Zoltowski, Brian Vaccaro & Brian R Crane
doi:10.1038/nchembio.210
Abstract - Mechanism-based tuning of a LOV domain photoreceptor | Full Text - Mechanism-based tuning of a LOV domain photoreceptor | PDF (837 KB) - Mechanism-based tuning of a LOV domain photoreceptor | Supplementary information | Chemical compounds
How curved membranes recruit amphipathic helices and protein anchoring motifs - pp835 - 841
Nikos S Hatzakis, Vikram K Bhatia, Jannik Larsen, Kenneth L Madsen, Pierre-Yves Bolinger, Andreas H Kunding, John Castillo, Ulrik Gether, Per Hedegård & Dimitrios Stamou
doi:10.1038/nchembio.213
Abstract - How curved membranes recruit amphipathic helices and protein anchoring motifs | Full Text - How curved membranes recruit amphipathic helices and protein anchoring motifs | PDF (1,259 KB) - How curved membranes recruit amphipathic helices and protein anchoring motifs | Supplementary information | Chemical compounds
Emergent bistability by a growth-modulating positive feedback circuit - pp842 - 848
Cheemeng Tan, Philippe Marguet & Lingchong You
doi:10.1038/nchembio.218
Abstract - Emergent bistability by a growth-modulating positive feedback circuit | Full Text - Emergent bistability by a growth-modulating positive feedback circuit | PDF (567 KB) - Emergent bistability by a growth-modulating positive feedback circuit | Supplementary information | Chemical compounds
Chemical genomics in Escherichia coli identifies an inhibitor of bacterial lipoprotein targeting - pp849 - 856
Ranjana Pathania, Soumaya Zlitni, Courtney Barker, Rahul Das, David A Gerritsma, Julie Lebert, Emilia Awuah, Giuseppe Melacini, Fred A Capretta & Eric D Brown
doi:10.1038/nchembio.221
Abstract - Chemical genomics in : Escherichia coli: identifies an inhibitor of bacterial lipoprotein targeting | Full Text - Chemical genomics in Escherichia coli identifies an inhibitor of bacterial lipoprotein targeting | PDF (1,210 KB) - Chemical genomics in Escherichia coli identifies an inhibitor of bacterial lipoprotein targeting | Supplementary information | Chemical compounds
The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo - pp857 - 862
Vincent Dupres, David Alsteens, Sabrina Wilk, Benjamin Hansen, Jürgen J Heinisch & Yves F Dufrêne
doi:10.1038/nchembio.220
Abstract - The yeast Wsc1 cell surface sensor behaves like a nanospring : in vivo | Full Text - The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo | PDF (591 KB) - The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo | Supplementary information
