@article {1165,
	title = {The structural and dynamic basis of Ets-1 DNA binding autoinhibition},
	journal = {Journal of Biological Chemistry},
	volume = {280},
	number = {8},
	year = {2005},
	note = {ISI Document Delivery No.: 902DTTimes Cited: 19Cited Reference Count: 73},
	month = {Feb},
	pages = {7088-7099},
	type = {Article},
	abstract = {The transcription factor Ets-1 is regulated by the allosteric coupling of DNA binding with the unfolding of an alpha-helix (HI-1) within an autoinhibitory module. To understand the structural and dynamic basis for this autoinhibition, we have used NAIR spectroscopy to characterize Ets-1DeltaN301, a partially inhibited fragment of Ets-1. The NMR-derived Ets-1DeltaN301 structure reveals that the autoinhibitory module is formed predominantly by the hydrophobic packing of helices from the N-terminal (HI-1, HI-2) and C-terminal (114, 115) inhibitory sequences, along with H1 of the intervening DNA binding ETS domain. The intramolecular interactions made by HI-1 in Ets-1DeltaN301 are similar to the intermolecular contacts observed in the crystal structure of an Ets-1DeltaN300 dimer, confirming that the latter represents a domain-swapped species. N-15 relaxation studies demonstrate that the backbone of the N-terminal inhibitory sequence is mobile on the nanosecond-picosecond and millisecond-microsecond time scales. Furthermore, hydrogen exchange measurements reveal that amide protons in helices HI-I and HI-2 exchange with water at rates only similar to15- and similar to75-fold slower, respectively, than predicted for an unfolded polypeptide. These findings indicate that inhibitory helices are only marginally stable even in the absence of DNA. The energetic coupling of DNA binding with the facile unfolding of the labile HI-1 provides a mechanism for modulating Ets-1 DNA binding activity via protein partnerships, post-translational modifications, or mutations. Ets-1 autoinhibition illustrates how conformational equilibria within structural domains can regulate macromolecular interactions.},
	keywords = {BACKBONE DYNAMICS, CHEMICAL-EXCHANGE, DIPOLAR COUPLINGS, Ets-1, GROUP HYDROGEN-EXCHANGE, HIGH-RESOLUTION, MURINE, N-15 NMR RELAXATION, POINTED DOMAIN, SECONDARY STRUCTURE, SIDE-CHAINS},
	isbn = {0021-9258},
	url = {<Go to ISI>://000227332700099},
	author = {Lee, G. M. and Donaldson, L. W. and Pufall, M. A. and Kang, H. S. and Pot, I. and Graves, B. J. and McIntosh, L. P.}
}
@article {728,
	title = {Identification and interpretation of generalized two-dimensional correlation spectroscopy features through decomposition of the perturbation domain},
	journal = {Applied Spectroscopy},
	volume = {57},
	number = {12},
	year = {2003},
	note = {ISI Document Delivery No.: 753MHTimes Cited: 8Cited Reference Count: 33},
	month = {Dec},
	pages = {1561-1574},
	type = {Article},
	abstract = {Generalized two-dimensional correlation spectroscopy offers great scope for revealing the behavior of relationships between components of a system under empirical study. We have developed methods that aid in the interpretation of two-dimensional correlation spectroscopy. These methods include reference patterns for two-dimensional correlation and correlation coefficient maps, their superposition and joint interpretation, and the use of delta functions to decompose them in the perturbation domain. We show how their joint use permits discrimination between similar two-dimensional correlation map features on the basis of different correlation coefficients. We also show how the decomposition of maps into the perturbation domain reflects the dynamic behavior of spectral features over the course of the perturbation and permits discrimination between otherwise highly similar two-dimensional correlation crosspeaks. These approaches simplify the interpretation of two-dimensional correlation spectroscopy maps and facilitate access to their rich information content.},
	keywords = {coefficient maps, COMPONENT ANALYSIS, correlation, FT-IR SPECTROSCOPY, INFRARED CORRELATION SPECTROSCOPY, INTENSITY CHANGES, MONOLAYER FILMS, perturbation domain decomposition, RAMAN-SPECTRA, reference patterns, SAMPLE-SAMPLE, SECONDARY STRUCTURE, SIMULATIONS, SPECTRA, trajectory peaks, two-dimensional correlation spectra},
	isbn = {0003-7028},
	url = {<Go to ISI>://000187234800014},
	author = {Schulze, G. and Jirasek, A. and Blades, M. W. and Turner, R. F. B.}
}
@article {728,
	title = {Identification and interpretation of generalized two-dimensional correlation spectroscopy features through decomposition of the perturbation domain},
	journal = {Applied Spectroscopy},
	volume = {57},
	number = {12},
	year = {2003},
	note = {ISI Document Delivery No.: 753MHTimes Cited: 8Cited Reference Count: 33},
	month = {Dec},
	pages = {1561-1574},
	type = {Article},
	abstract = {Generalized two-dimensional correlation spectroscopy offers great scope for revealing the behavior of relationships between components of a system under empirical study. We have developed methods that aid in the interpretation of two-dimensional correlation spectroscopy. These methods include reference patterns for two-dimensional correlation and correlation coefficient maps, their superposition and joint interpretation, and the use of delta functions to decompose them in the perturbation domain. We show how their joint use permits discrimination between similar two-dimensional correlation map features on the basis of different correlation coefficients. We also show how the decomposition of maps into the perturbation domain reflects the dynamic behavior of spectral features over the course of the perturbation and permits discrimination between otherwise highly similar two-dimensional correlation crosspeaks. These approaches simplify the interpretation of two-dimensional correlation spectroscopy maps and facilitate access to their rich information content.},
	keywords = {coefficient maps, COMPONENT ANALYSIS, correlation, FT-IR SPECTROSCOPY, INFRARED CORRELATION SPECTROSCOPY, INTENSITY CHANGES, MONOLAYER FILMS, perturbation domain decomposition, RAMAN-SPECTRA, reference patterns, SAMPLE-SAMPLE, SECONDARY STRUCTURE, SIMULATIONS, SPECTRA, trajectory peaks, two-dimensional correlation spectra},
	isbn = {0003-7028},
	url = {<Go to ISI>://000187234800014},
	author = {Schulze, G. and Jirasek, A. and Blades, M. W. and Turner, R. F. B.}
}
@article {648,
	title = {Revealing system dynamics through decomposition of the perturbation domain in two-dimensional correlation spectroscopy},
	journal = {Applied Spectroscopy},
	volume = {57},
	number = {12},
	year = {2003},
	note = {ISI Document Delivery No.: 753MHTimes Cited: 5Cited Reference Count: 36},
	month = {Dec},
	pages = {1551-1560},
	type = {Article},
	abstract = {A technique is presented to simply and effectively decompose the perturbation domain in two-dimensional (2D) correlation maps calculated on a given set of vibrational spectra. Decomposition of the perturbation domain exposes a wealth of kinetic information complementary to the information extracted from conventional 2D correlation spectroscopy. It is shown that the technique produces "perturbation profile maps" that can be utilized in both the interpretation of the conventional 2D correlation maps and the independent kinetic analysis of the given system. Discrimination between spectral features exhibiting similar, but not identical, dynamics is facilitated by the decomposition, and spectral features exhibiting identical dynamics over the perturbation interval are quickly identified. Spectral features exhibiting similar dynamics over only a sub-range of the full perturbation are also identifiable. Interpretation of phase information illuminated in synchronous and asynchronous maps is simplified. Comparison between similar spectral features present in different samples is facilitated with the technique. The simplicity and ease of implementation of the technique make decomposition of the perturbation domain a valuable addition to the tools available in 2D correlation analysis.},
	keywords = {cross-correlation, FT-RAMAN, HUMAN, INFRARED CORRELATION SPECTROSCOPY, multivariate data, POLYACRYLAMIDE GELS, POLYMER GEL DOSIMETERS, RADIATION-DOSIMETRY, Raman spectroscopy, SAMPLE-SAMPLE, SECONDARY STRUCTURE, SERUM-ALBUMIN, SPECTRA, STRUCTURAL-CHANGES, two-dimensional correlation spectroscopy},
	isbn = {0003-7028},
	url = {<Go to ISI>://000187234800013},
	author = {Jirasek, A. and Schulze, G. and Blades, M. W. and Turner, R. F. B.}
}
@article {648,
	title = {Revealing system dynamics through decomposition of the perturbation domain in two-dimensional correlation spectroscopy},
	journal = {Applied Spectroscopy},
	volume = {57},
	number = {12},
	year = {2003},
	note = {ISI Document Delivery No.: 753MHTimes Cited: 5Cited Reference Count: 36},
	month = {Dec},
	pages = {1551-1560},
	type = {Article},
	abstract = {A technique is presented to simply and effectively decompose the perturbation domain in two-dimensional (2D) correlation maps calculated on a given set of vibrational spectra. Decomposition of the perturbation domain exposes a wealth of kinetic information complementary to the information extracted from conventional 2D correlation spectroscopy. It is shown that the technique produces "perturbation profile maps" that can be utilized in both the interpretation of the conventional 2D correlation maps and the independent kinetic analysis of the given system. Discrimination between spectral features exhibiting similar, but not identical, dynamics is facilitated by the decomposition, and spectral features exhibiting identical dynamics over the perturbation interval are quickly identified. Spectral features exhibiting similar dynamics over only a sub-range of the full perturbation are also identifiable. Interpretation of phase information illuminated in synchronous and asynchronous maps is simplified. Comparison between similar spectral features present in different samples is facilitated with the technique. The simplicity and ease of implementation of the technique make decomposition of the perturbation domain a valuable addition to the tools available in 2D correlation analysis.},
	keywords = {cross-correlation, FT-RAMAN, HUMAN, INFRARED CORRELATION SPECTROSCOPY, multivariate data, POLYACRYLAMIDE GELS, POLYMER GEL DOSIMETERS, RADIATION-DOSIMETRY, Raman spectroscopy, SAMPLE-SAMPLE, SECONDARY STRUCTURE, SERUM-ALBUMIN, SPECTRA, STRUCTURAL-CHANGES, two-dimensional correlation spectroscopy},
	isbn = {0003-7028},
	url = {<Go to ISI>://000187234800013},
	author = {Jirasek, A. and Schulze, G. and Blades, M. W. and Turner, R. F. B.}
}
@article {389,
	title = {The solution structure and interactions of CheW from Thermotoga maritima},
	journal = {Nature Structural Biology},
	volume = {9},
	number = {2},
	year = {2002},
	note = {ISI Document Delivery No.: 516PHTimes Cited: 35Cited Reference Count: 34},
	month = {Feb},
	pages = {121-125},
	type = {Article},
	abstract = {Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.},
	keywords = {BACTERIAL CHEMOTAXIS, BINDING DOMAIN, C-13-LABELED PROTEINS, ESCHERICHIA-COLI, HISTIDINE KINASE, KINASE CHEA, NMR EXPERIMENTS, RESONANCE ASSIGNMENTS, SECONDARY STRUCTURE, SIGNAL-TRANSDUCTION},
	isbn = {1072-8368},
	url = {<Go to ISI>://000173562000015},
	author = {Griswold, I. J. and Zhou, H. J. and Matison, M. and Swanson, R. V. and McIntosh, L. P. and Simon, M. I. and Dahlquist, F. W.}
}
@article {3800,
	title = {Secondary structure and NMR assignments of Bacillus circulans xylanase},
	journal = {Protein Science},
	volume = {5},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UP617Times Cited: 23Cited Reference Count: 74},
	month = {Jun},
	pages = {1118-1135},
	type = {Article},
	abstract = {Bacillus circulans xylanase (BCX) is a member of the family of low molecular weight endo-beta-(1,4)-xylanases. The main-chain H-1, C-13, and N-15 resonances of this 20.4-kDa enzyme were assigned using heteronuclear NMR experiments recorded on a combination of selectively and uniformly labeled protein samples. Using chemical shift, NOE, J coupling, and amide hydrogen exchange information, 14 beta-strands, arranged in a network of three beta-sheets, and a single cy-helix were identified in BCX. The NMR-derived secondary structure and beta-sheet topology agree closely with that observed in the crystal structure of this protein. The H-N of Ile 118 has a strongly upfield-shifted resonance at 4.03 ppm, indicative of a potential amide-aromatic hydrogen bond to the indole ring of Trp 71. This interaction, which is conserved in all low molecular weight xylanases of known structure, may play an important role in establishing the active site conformation of these enzymes. Following hen egg white and bacteriophage T4 lysozymes, B. circulans xylanase represents the third family of beta-glycanases for which extensive NMR assignments have been reported. These assignments provide the background for detailed studies of the mechanism of carbohydrate recognition and hydrolysis by this bacterial xylanase.},
	keywords = {amide-aromatic hydrogen bond, AMINO-ACID, ASSIGNMENTS, BACKBONE AMIDE, beta-glycanase, C-13-LABELED PROTEINS, C-ALPHA, chemical shift index, CHEMICAL-SHIFTS, COUPLING-CONSTANTS, LARGER PROTEINS, NMR, NUCLEAR-MAGNETIC-RESONANCE, SECONDARY STRUCTURE, SIDE-CHAIN RESONANCES, SOLVENT, SUPPRESSION, XYLANASE},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996UP61700014},
	author = {Plesniak, L. A. and Wakarchuk, W. W. and McIntosh, L. P.}
}
@article {2925,
	title = {CIRCULAR-DICHROISM ANALYSIS OF A SYNTHETIC PEPTIDE CORRESPONDING TO THE ALPHA,ALPHA-CORNER MOTIF OF HEMOGLOBIN},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {196},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: MC105Times Cited: 1Cited Reference Count: 16},
	month = {Oct},
	pages = {435-439},
	type = {Article},
	keywords = {ALPHA-HELIX, GLOBULAR-PROTEINS, INTERMEDIATE, POLYPEPTIDE-CHAIN, SECONDARY STRUCTURE, STABILITY},
	isbn = {0006-291X},
	url = {<Go to ISI>://A1993MC10500062},
	author = {Tsai, F. C. S. and Sherman, J. C.}
}
