@article {2493,
	title = {Total Synthesis and Stereochemical Assignment of Micrococcin P1},
	journal = {Angewandte Chemie-International Edition},
	volume = {48},
	number = {23},
	year = {2009},
	note = {ISI Document Delivery No.: 452GHTimes Cited: 11Cited Reference Count: 41Lefranc, David Ciufolini, Marco A.},
	pages = {4198-4201},
	type = {Article},
	keywords = {ACID, antibiotics, CHEMISTRY, DOMAIN, FRAGMENT A-C, GE2270-A, HETEROCYCLES, MICROCOCCIN P1, P-1, PROTEIN-SYNTHESIS, THIOPEPTIDE ANTIBIOTICS, thiopeptides, THIOSTREPTON},
	isbn = {1433-7851},
	url = {<Go to ISI>://000266527800024},
	author = {Lefranc, D. and Ciufolini,Marco A.}
}
@article {2141,
	title = {The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region},
	journal = {Journal of Molecular Biology},
	volume = {382},
	number = {4},
	year = {2008},
	note = {ISI Document Delivery No.: 359YPTimes Cited: 3Cited Reference Count: 42Lee, Gregory M. Pufall, Miles A. Meeker, Charles A. Kang, Hyun-Seo Graves, Barbara J. McIntosh, Lawrence P.},
	month = {Oct},
	pages = {1014-1030},
	type = {Article},
	abstract = {Binding of the transcription factor Ets-1 to DNA is allosterically regulated by a serine-rich region (SRR) that modulates the dynamic character of the adjacent structured DNA-binding ETS domain and its flanking autoinhibitory elements. Multi-site phosphorylation of the flexible SRR in response to Ca2+ signaling mediates variable regulation of Ets-1 DNA-binding affinity. In this study, we further investigated the mechanism of this regulation. First, thermal and urea denaturation experiments demonstrated that phosphorylation of the predominantly unstructured SRR imparts enhanced thermodynamic stability on the well-folded ETS domain and its inhibitory module. We next identified a minimal fragment (residues 279-440) that exhibits both enhanced autoinhibition of Ets-1 DNA-binding and allosteric reinforcement by phosphorylation. To test for intramolecular interactions between the SRR and the rest of the fragment that were not detectable by H-1-H-1 NOE measurements, paramagnetic relaxation enhancements were performed using Cu2+ bound to the N-terminal ATCUN motif. Increased relaxation detected for specific amide and methyl groups revealed a preferential interaction surface for the flexible SRR extending from the inhibitory module to the DNA-binding interface. Phosphorylation enhanced the localization of the SRR to this surface. We therefore hypothesize that the positioning of the SRR at the DNA-binding interface and its role in shifting Ets-1 to an inhibited conformation are linked. In particular, transient interactions dampen the conformational flexibility of the ETS domain and inhibitory module required for high-affinity binding, as well as possibly occlude the DNA interaction site. Surprisingly, the phosphorylation-dependent effects were relatively insensitive to changes in ionic strength, suggesting that electrostatic forces are not the dominant mechanism for mediating these interactions. The results of this study highlight the role of flexibility and transient binding in the variable regulation of Ets-1 activity. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {allosteric regulation, ATCUN MOTIF, AUTOINHIBITION, BINDING, CHEMICAL-SHIFTS, DISORDERED PROTEIN, DOMAIN, DYNAMICS, GROUP HYDROGEN-EXCHANGE, NMR, paramagnetic relaxation, PARAMAGNETIC RELAXATION ENHANCEMENT, protein dynamics, SPECTROSCOPY, transcription},
	isbn = {0022-2836},
	url = {<Go to ISI>://000260024500017},
	author = {Lee, G. M. and Pufall, M. A. and Meeker, C. A. and Kang, H. S. and Graves, B. J. and McIntosh, L. P.}
}
@article {2035,
	title = {Protein-protein interaction regulates proteins{\textquoteright} mechanical stability},
	journal = {Journal of Molecular Biology},
	volume = {378},
	number = {5},
	year = {2008},
	note = {ISI Document Delivery No.: 305IOTimes Cited: 10Cited Reference Count: 38Cao, Yi Yoo, Teri Zhuang, Shulin Li, Hongbin},
	month = {May},
	pages = {1132-1141},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs found not only in a variety of biological machines and tissues, but also in biomaterials of superb mechanical properties. Regulating the mechanical stability of elastomeric proteins is not only important for a range of biological processes, but also critical for the use of engineered elastomeric proteins as building blocks to construct nanomechanical devices and novel materials of well-defined mechanical properties. Here we demonstrate that protein-protein interactions can potentially serve as an effective means to regulate the mechanical properties of elastomeric proteins. We show that the binding of fragments of IgG antibody to a small protein, GB1, can significantly enhance the mechanical stability of GB1. The regulation of the mechanical stability of GB1 by IgG fragments is not through direct modification of the interactions in the mechanically key region of GB1; instead, it is accomplished via the long-range coupling between the IgG binding site and the mechanically key region of GB1. Although Fc and Fab bind GB1 at different regions of GB1, their binding to GB1 can increase the mechanical stability of GB1 significantly. Using alanine point mutants of GB1, we show that the amplitude of mechanical stability enhancement of GB1 by Fc does not correlate with the binding affinity, suggesting that binding affinity only affects the population of GB1/human Fc (hFc) complex at a given concentration of hFc, but does not affect the intrinsic mechanical stability of the GB1/hFc complex. Furthermore, our results indicate that the mechanical stability enhancement by IgG fragments is robust and can tolerate sequence/structural perturbation to GB1. Our results demonstrate that the protein-protein interaction is an efficient approach to regulate the mechanical stability of GB1-like proteins and we anticipate that this new methodology will help to develop novel elastomeric proteins with tunable mechanical stability and compliance. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BINDING, BIOLOGICAL ROLES, CRYSTAL-STRUCTURE, DIHYDROFOLATE-REDUCTASE, DOMAIN, ENGINEERING PROTEINS, FORCE SPECTROSCOPY, FRAGMENT, HUMAN-IGG, MECHANICAL STABILITY, mechanical unfolding, MOLECULAR ELASTICITY, protein-protein interaction, single molecule atomic force microscopy, STABILIZATION},
	isbn = {0022-2836},
	url = {<Go to ISI>://000256171900015},
	author = {Cao, Y. and Yoo, T. and Zhuang, S. L. and Li, H. B.}
}
@article {2235,
	title = {Sintokamides A to E, Chlorinated Peptides from the Sponge Dysidea sp that Inhibit Transactivation of the N-Terminus of the Androgen Receptor in Prostate Cancer Cells},
	journal = {Organic Letters},
	volume = {10},
	number = {21},
	year = {2008},
	note = {ISI Document Delivery No.: 367EETimes Cited: 10Cited Reference Count: 23Sadar, Marianne D. Williams, David E. Mawji, Nasrin R. Patrick, Brian O. Wikanta, Thamrin Chasanah, Ekowati Irianto, Hari Eko Van Soest, Rob Andersen, Raymond J.},
	month = {Nov},
	pages = {4947-4950},
	type = {Article},
	abstract = {The new chlorinated peptides sintokamides A to E (1-5) have been isolated from specimens of the marine sponge Dysidea sp. collected in Indonesia. Their structures were elucidated by a combination of spectroscopic and single-crystal X-ray diffraction analyses. Sintokamide A (1) is an inhibitor of N-terminus transactivation of the androgen receptor in prostate cancer cells.},
	keywords = {AMINO-ACID, BARBAMIDE, biosynthesis, CYANOBACTERIUM, DOMAIN, HERBACEA, METABOLITES},
	isbn = {1523-7060},
	url = {<Go to ISI>://000260534500060},
	author = {Sadar, M. D. and Williams, D. E. and Mawji, N. R. and Patrick, B. O. and Wikanta, T. and Chasanah, E. and Irianto, H. E. and Van Soest, R. and Andersen, R. J.}
}
@article {1545,
	title = {Characterization of de novo four-helix bundles by molecular dynamics simulations},
	journal = {Proteins-Structure Function and Bioinformatics},
	volume = {64},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 064QITimes Cited: 5Cited Reference Count: 34Scott, Walter R. P. Seo, Emily Huttunen, Heidi Wallhorn, Diana Sherman, John C. Straus, Suzana K.},
	month = {Aug},
	pages = {719-729},
	type = {Article},
	abstract = {We have investigated the structure and dynamics of three cavitand-based four-helix bundles (caviteins) by computer simulation. In these systems, designed de novo, each of the four helices contain the identical basis sequence EELLKKLEELLKKG (N1). Each cavitein consists of a rigid macrocycle (cavitand) with four aryl linkages, to each of which is connected an NI peptide by means of a linker peptide. The three caviteins studied here differ only in the linker peptide, which consist of one, two, or three glycine residues. Previous experimental work has shown that these systems exhibit very different behavior in terms of stability and oligomerization states despite the small differences in the linker peptide. Given that to date no three-dimensional structure is available for these caviteins, we have undertaken a series of molecular dynamics (MD) simulations in explicit water to try to rationalize the large differences in the experimentally observed behavior of these systems. Our results provide insight, for the first time, into why and how the cavitein with a single glycine linker forms dimers. In addition, our results indicate why although the two- and three-glycine-linked caviteins have similar stabilities, they have different native-like characteristics: the cavitein with three glycines can form a supercoiled helix, whereas the one with two glycines cannot. These findings may provide a useful guide in the rational de novo design of novel proteins with finely tunable structures and functions in the future.},
	keywords = {caviteins, de novo four-helix bundle, DESIGN, DOMAIN, HELICAL BUNDLES, molecular dynamics simulations, PEPTIDE, PROTEIN DESIGN, PROTEINS, STATE, SYSTEM, TASP, template-assembled synthetic protein},
	isbn = {0887-3585},
	url = {<Go to ISI>://000239103800014},
	author = {Scott, W. R. P. and Seo, E. and Huttunen, H. and Wallhorn, D. and Sherman, J. C. and Straus, S. K.}
}
@article {1612,
	title = {The structure of gelsolin bound to ATP},
	journal = {Journal of Molecular Biology},
	volume = {357},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 030IYTimes Cited: 7Cited Reference Count: 28},
	month = {Mar},
	pages = {765-772},
	type = {Article},
	abstract = {Calcium activation of the actin-modifying properties of gelsolin is sensitive to ATP. Here, we show that soaking calcium-free gelsolin crystals in ATP-containing media results in ATP occupying a site that spans the two pseudosymmetrical halves of the protein. ATP binding involves numerous polar and hydrophobic contacts and is identical for the two copies of gelsolin related by non-crystallographic symmetry within the crystal. The gamma-phosphate of ATP participates in several charge-charge interactions consistent with the preference of gelsolin for ATP, as a binding partner, over ADP. In addition, disruption of the ATP-binding site through Ca2+ activation of gelsolin reveals why ATP binds more tightly to the inactive molecule, and suggests how the binding of ATP may modulate the sensitivity of gelsolin to calcium ions. Similarities between the ATP and PIP2 interactions with the C-terminal half of gelsolin are evident from their overlapping binding sites and in that both molecules bind more tightly in the absence of calcium ions. We propose a model for how PIP2 may bind to calcium-free gelsolin based on the ATP-binding site. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {5-BISPHOSPHATE, actin, ATP, BINDING-SITE, calcium, CRYSTAL-STRUCTURE, DOMAIN, gelsolin, HUMAN-PLASMA GELSOLIN, IDENTIFICATION, PHOSPHATIDYLINOSITOL 4, PIP2, PROTEIN, TERMINAL HALF},
	isbn = {0022-2836},
	url = {<Go to ISI>://000236629300007},
	author = {Urosev, D. and Ma, Q. and Tan, A. L. C. and Robinson, R. C. and Burtnick, L. D.}
}
@article {1621,
	title = {The unfolding and folding dynamics of TNfnALL probed by single molecule force-ramp spectroscopy},
	journal = {Polymer},
	volume = {47},
	number = {7},
	year = {2006},
	note = {ISI Document Delivery No.: 030JETimes Cited: 10Cited Reference Count: 53},
	month = {Mar},
	pages = {2548-2554},
	type = {Article},
	abstract = {Tenascin, an important extracellular matrix protein, is subject to stretching force under physiological conditions and plays important roles in regulating the cell-matrix interactions. Using the recently developed single molecule force-ramp spectroscopy, we investigated the unfolding-folding kinetics of a recombinant tenascin fragment TNfnALL. Our results showed that all the 15 FnIII domains in TNfnALL have similar spontaneous unfolding rate constant at zero force, but show great difference in their folding rate constants. Our results demonstrated that single molecule force-ramp spectroscopy is a powerful tool for accurate determination of the kinetic parameters that characterize the unfolding and folding reactions. We anticipate that single molecule force-ramp spectroscopy will become a versatile addition to the single molecule manipulation tool box and greatly expand the scope of single molecule force spectroscopy. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {ADHESION, DOMAIN, EXPRESSION, III, IMMUNOGLOBULIN, MATRIX PROTEINS, MECHANICAL STABILITY, microscopy, MUSCLE PROTEIN TITIN, tenascin, UBIQUITIN},
	isbn = {0032-3861},
	url = {<Go to ISI>://000236629900037},
	author = {Wang, M. J. and Cao, Y. and Li, H. B.}
}
@article {1063,
	title = {Can PISEMA experiments be used to extract structural parameters for mobile beta-barrels?},
	journal = {Journal of Biomolecular Nmr},
	volume = {32},
	number = {2},
	year = {2005},
	note = {ISI Document Delivery No.: 948CRTimes Cited: 4Cited Reference Count: 42},
	month = {Jun},
	pages = {101-111},
	type = {Article},
	abstract = {The effect of mobility on N-15 chemical shift/N-15-H-1 dipolar coupling (PISEMA) solid state NMR experiments applied to macroscopically oriented beta-barrels is assessed using molecular dynamics simulation data of the NalP autotransporter domain embedded in a DMPC bilayer. In agreement with previous findings for alpha-helices, the fast librational motion of the peptide planes is found to have a considerable effect on the calculated PISEMA spectra. In addition, the dependence of the chemical shift anisotropy (CSA) and dipolar coupling parameters on the calculated spectra is evaluated specifically for the beta-barrel case. It is found that the precise choice of the value of the CSA parameters sigma(11), sigma(22) and sigma(33) has only a minor effect, whereas the choice of the CSA parameter theta shifts the position of the peaks by up to 20 ppm and changes the overall shape of the spectrum significantly. As was found for alpha-helices, the choice of the NH bond distance has a large effect on the dipolar coupling constant used for the calculations. Overall, it is found that the alternating beta-strands in the barrel occupy distinct regions of the PISEMA spectra, forming patterns which may prove useful in peak assignment.},
	keywords = {ANGLE-SPINNING NMR, ASSIGNMENT, COAT PROTEIN, CONSTRAINTS, DOMAIN, HELICAL WHEELS, MEMBRANE-PROTEINS, mobility of membrane beta-barrels, MOLECULAR-DYNAMICS SIMULATIONS, mosaic spread, PISEMA, SOLID-STATE NMR, SPECTROSCOPY, time averaging},
	isbn = {0925-2738},
	url = {<Go to ISI>://000230694100001},
	author = {Bleile, D. W. and Scott, W. R. P. and Straus, S. K.}
}
@article {1053,
	title = {The state of the filament},
	journal = {Embo Reports},
	volume = {6},
	number = {3},
	year = {2005},
	note = {ISI Document Delivery No.: 901QMTimes Cited: 22Cited Reference Count: 30},
	month = {Mar},
	pages = {220-226},
	type = {Review},
	abstract = {Movement is a defining characteristic of life. Macroscopic motion is driven by the dynamic interactions of myosin with actin filaments in muscle. Directed polymerization of actin behind the advancing membrane of a eukaryotic cell generates microscopic movement. Despite the fundamental importance of actin in these processes, the structure of the actin filament remains unknown. The Holmes model of the actin filament was published 15 years ago, and although it has been widely accepted, no high-resolution structural data have yet confirmed its veracity. Here, we review the implications of recently determined structures of F-actin-binding proteins for the structure of the actin filament and suggest a series of in silico tests for actin-filament models. We also review the significance of these structures for the arp2/3-mediated branched filament.},
	keywords = {actin filament, ACTIN-FILAMENT, ACTIVATION, ALDRICH-SYNDROME PROTEIN, arp2/3, ARP2/3 COMPLEX, BETA-ACTIN, CRYSTAL-STRUCTURE, DOMAIN, gelsolin, STRUCTURAL BASIS, STRUCTURE, WASp, WH2},
	isbn = {1469-221X},
	url = {<Go to ISI>://000227297000009},
	author = {Aguda, A. H. and Burtnick, L. D. and Robinson, R. C.}
}
@article {1233,
	title = {Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region},
	journal = {Science},
	volume = {309},
	number = {5731},
	year = {2005},
	note = {ISI Document Delivery No.: 941KDTimes Cited: 66Cited Reference Count: 30},
	month = {Jul},
	pages = {142-145},
	type = {Article},
	abstract = {Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.},
	keywords = {allosteric regulation, AUTOINHIBITION, DOMAIN, DYNAMICS, NMR-SPECTROSCOPY, PHOSPHORYLATION, PROTEIN, SITES, TRANSACTIVATION, TRANSCRIPTION FACTOR NFAT1},
	isbn = {0036-8075},
	url = {<Go to ISI>://000230212800079},
	author = {Pufall, M. A. and Lee, G. M. and Nelson, M. L. and Kang, H. S. and Velyvis, A. and Kay, L. E. and McIntosh, L. P. and Graves, B. J.}
}
@article {444,
	title = {Carbohydrate-binding modules recognize fine substructures of cellulose},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {52},
	year = {2002},
	note = {ISI Document Delivery No.: 631QDTimes Cited: 20Cited Reference Count: 36},
	month = {Dec},
	pages = {50245-50254},
	type = {Article},
	abstract = {Competition isotherms are used to identify the set of cellulose substructures to which cellulose binding modules (CBMs) from families 2a, 3, 4, 9, and 17 bind. The experiments are based on coupling a unique fluorescent tag to each CBM in a manner that does not alter the natural binding properties of the CBM and therefore allows the surface and solution concentrations of each CBM to be monitored as a function of time and composition. Adsorption and surface exchange of like or competing CBMs are monitored using a range of cellulose preparations varying in both crystallinity and provenance. CBMs from families 2a, 3,4,9, and 17 are shown to recognize different physical forms of prepared cellulose. The demonstration of the very fine binding specificity of cellulose-specific CBMs implies that the polysaccharide targets of CBMs extend down to the resolution of cellulose microstructures.},
	keywords = {BACTERIAL, CELLULASE, CRYSTALLINE CELLULOSE, DOMAIN, EXOGLUCANASE, FIMI CENC, NMR-SPECTROSCOPY, PROTEIN-A, SPECIFICITY, TRYPTOPHAN RESIDUES, XYLANASE 10A},
	isbn = {0021-9258},
	url = {<Go to ISI>://000180177700007},
	author = {McLean, B. W. and Boraston, A. B. and Brouwer, D. and Sanaie, N. and Fyfe, C. A. and Warren, R. A. J. and Kilburn, D. G. and Haynes, C. A.}
}
@article {541,
	title = {Inhibitory module of Ets-1 allosterically regulates DNA binding through a dipole-facilitated phosphate contact},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {3},
	year = {2002},
	note = {ISI Document Delivery No.: 514CWTimes Cited: 21Cited Reference Count: 50},
	month = {Jan},
	pages = {2225-2233},
	type = {Article},
	abstract = {DNA binding of the transcription factor Ets-1 is negatively regulated by three inhibitory helices that lie near the ETS domain. The current model suggests that this negative regulation, termed autoinhibition, is caused by the energetic expense of a DNA-induced structural transition that includes the unfolding of one inhibitory helix. This report investigates the role of helix H1 of the ETS domain in the autoinhibition mechanism. Previous structural studies modeled the inhibitory helices packing together and connecting with helix H1, suggesting a role of this helix in the configuration of an inhibitory module. Recently, high-resolution structures of the ETS domain-DNA interface indicate that the N terminus of helix H1 directly contacts DNA. The contact, which is augmented by the macrodipole of helix H1, consists of a hydrogen bond between the amide NH of leucine 337 in helix HI and the oxygen of a corresponding phosphate. We propose that this hydrogen bond positions helix H1 to be a link between autoinhibition and DNA binding. Four independent approaches tested this hypothesis. First, the hydrogen bond was disrupted by removal of the phosphate in a missing phosphate analysis. Second, base pairs that surround the helix HI-contacting phosphate and appear to dictate DNA backbone conformation were mutated. Next, a hydrophobic residue in helix H1 that is expected to position the N terminus of the helix was altered. Finally, a residue on the surface of helix 111 that may contact the inhibitory elements was changed. In each case DNA binding and autoinhibition was affected. Taken together, the results demonstrate the role of the dipole-facilitated phosphate contact in DNA binding. Furthermore, the findings support a model in which helix H1 links the inhibitory elements to the ETS domain. We speculate that this helix, which is conserved in all Ets proteins, provides a common route to regulation.},
	keywords = {ALPHA-HELIX, AUTO-INHIBITION, COMPLEX, DOMAIN, FACTORS ELK-1, INDIRECT READOUT, MURINE ETS-1, PROTEINS, RECOGNITION, TRANSCRIPTION FACTOR},
	isbn = {0021-9258},
	url = {<Go to ISI>://000173421300083},
	author = {Wang, H. and McIntosh, L. P. and Graves, B. J.}
}
@article {558,
	title = {An NMR approach to structural proteomics},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {99},
	number = {4},
	year = {2002},
	note = {ISI Document Delivery No.: 524UKTimes Cited: 109Cited Reference Count: 28},
	month = {Feb},
	pages = {1825-1830},
	type = {Article},
	abstract = {The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMIR. Although there was variability among proteomes, overall 20\% of these proteins were found to be readily amenable to NMR structure determination. NMIR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.},
	keywords = {ASSIGNMENTS, CATH, DOMAIN, PROGRAM, PROTEINS, SPECTRA},
	isbn = {0027-8424},
	url = {<Go to ISI>://000174031100016},
	author = {Yee, A. and Chang, X. Q. and Pineda-Lucena, A. and Wu, B. and Semesi, A. and Le, B. and Ramelot, T. and Lee, G. M. and Bhattacharyya, S. and Gutierrez, P. and Denisov, A. and Lee, C. H. and Cort, J. R. and Kozlov, G. and Liao, J. and Finak, G. and Chen, L. and Wishart, D. and Lee, W. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {5123,
	title = {Letter to the Editor: NMR-based structure of the conserved protein MTH865 from the Archaeon Methanobacterium thermoautotrophicum},
	journal = {Journal of Biomolecular Nmr},
	volume = {21},
	number = {1},
	year = {2001},
	note = {ISI Document Delivery No.: 475DETimes Cited: 1Cited Reference Count: 15},
	month = {Sep},
	pages = {63-66},
	type = {Article},
	keywords = {ALIGNMENT, DOMAIN, helical bundle, HETERONUCLEAR NMR, Methanobacterium, NOES, structural proteomics, thermoautotrophicum},
	isbn = {0925-2738},
	url = {<Go to ISI>://000171145900006},
	author = {Lee, G. M. and Edwards, A. M. and Arrowsmith, C. H. and McIntosh, L. P.}
}
@article {4873,
	title = {Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {97},
	number = {12},
	year = {2000},
	note = {ISI Document Delivery No.: 322UATimes Cited: 14Cited Reference Count: 34},
	month = {Jun},
	pages = {6316-6321},
	type = {Article},
	abstract = {The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast, Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three cu-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX2CXnCC sequence motif and serves to bridge an N-terminal loop with helix 3, This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.},
	keywords = {ABC10-BETA, ARCHAEA, COMMON SUBUNITS, DOMAIN, genomics, IN-VITRO, PROTEINS, RESOLUTION, SEQUENCE, transcription},
	isbn = {0027-8424},
	url = {<Go to ISI>://000087526300018},
	author = {Mackereth, C. D. and Arrowsmith, C. H. and Edwards, A. M. and McIntosh, L. P.}
}
@article {4235,
	title = {Characterization of a buried neutral histidine in Bacillus circulans xylanase: Internal dynamics and interaction with a bound water molecule},
	journal = {Biochemistry},
	volume = {37},
	number = {7},
	year = {1998},
	note = {ISI Document Delivery No.: YZ886Times Cited: 13Cited Reference Count: 59},
	month = {Feb},
	pages = {1810-1818},
	type = {Article},
	abstract = {NMR spectroscopy was used to characterize the dynamic behavior of His149 in Bacillus circulans xylanase (BCX) and its interaction with an internal water molecule. Rate constants for the specific acid-and base-catalyzed exchange following bimolecular kinetics (EX2) of the nitrogen-bonded H-epsilon 2 of this buried, neutral histidine were determined, At pD(min) 7.0 and 30 degrees C, the lifetime for this proton is 9.9 h, corresponding to a protection factor of similar to 10(7) relative to that predicted for an exposed histidine, The apparent activation energies measured for specific acid and base catalysis (7.0 and 17.4 kcal/mol) indicate that exchange occurs via local structural fluctuations. Consistent with its buried environment, the N-epsilon 2-H bond vector of His149 shows restricted mobility, as evidenced by an order parameter S-2 = 0.83 determined from N-15 relaxation measurements, The crystal structure of BCX reveals that a conserved, buried water hydrogen-bonds to the H-epsilon 2 of His149. Strong support for this interaction in solution is provided by the observation of a negative nuclear Overhauser effect (NOE) and positive rotating-frame Overhauser effect (ROE) between His149 H-epsilon 2 and a water molecule with the same chemical shift as the bulk solvent. However, the chemical shift of H-epsilon 2 (12.2 ppm) and a D/H fractionation factor close to unity (0.89 +/- 0.02) indicate that this is nor a so-called low-barrier hydrogen bond. Lower and upper bounds on the lifetime of the internal water are estimated to be 10(-8) and 10(-3) s. Therefore the chemical exchange of solvent protons with those of His149 H-epsilon 2 and the diffusion or physical exchange of the internal water to which the histidine is hydrogen-bonded differ in rate by over 7 orders of magnitude.},
	keywords = {ACTIVE-SITE, AMIDE PROTON-EXCHANGE, ASSIGNMENTS, DOMAIN, HYDROGEN-BOND, NMR-SPECTROSCOPY, NUCLEAR MAGNETIC-RESONANCE, PROTEINS, relaxation, TRICHODERMA-REESEI},
	isbn = {0006-2960},
	url = {<Go to ISI>://000072304200010},
	author = {Connelly, G. P. and McIntosh, L. P.}
}
@article {3478,
	title = {MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX},
	journal = {Science},
	volume = {269},
	number = {5232},
	year = {1995},
	note = {ISI Document Delivery No.: RX194Times Cited: 143Cited Reference Count: 49},
	month = {Sep},
	pages = {1866-1869},
	type = {Article},
	abstract = {Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an cr helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.},
	keywords = {BASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS},
	isbn = {0036-8075},
	url = {<Go to ISI>://A1995RX19400036},
	author = {Petersen, J. M. and Skalicky, J. J. and Donaldson, L. W. and McIntosh, L. P. and Alber, T. and Graves, B. J.}
}
