Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings.
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S. Grzesiek | T. Kiefhaber | S. Meier | Sebastian Meier | Stephan Grzesiek | Thomas Kiefhaber | Sarah Güthe | Sarah Güthe
[1] V. Muñoz,et al. Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation. , 2001, Journal of molecular biology.
[2] Christopher D. Kroenke,et al. The Static Magnetic Field Dependence of Chemical Exchange Linebroadening Defines the NMR Chemical Shift Time Scale , 2000 .
[3] H. Wennerström. Nuclear magnetic relaxation induced by chemical exchange , 1972 .
[4] M G Rossmann,et al. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. , 1997, Structure.
[5] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[6] D. Shortle,et al. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea , 2001, Science.
[7] S. Grzesiek,et al. Direct Observation of Hydrogen Bonds in Proteins by Interresidue 3hJNC' Scalar Couplings , 1999 .
[8] E. Terzaghi,et al. The role of the collar/whisker complex in bacteriophage T4D tail fiber attachment. , 1979, Journal of molecular biology.
[9] A. Annila,et al. Alignment of chain-like molecules , 2004, Journal of biomolecular NMR.
[10] E. Becker,et al. Calibration of methanol and ethylene glycol nuclear magnetic resonance thermometers , 1979 .
[11] R. Kammerer,et al. Stabilization of short collagen-like triple helices by protein engineering. , 2001, Journal of molecular biology.
[12] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity , 1982 .
[13] F. Eiserling,et al. Studies on the structure, protein composition and aseembly of the neck of bacteriophage T4. , 1977, Journal of molecular biology.
[14] Ad Bax,et al. Flexibility and function in HIV-1 protease , 1995, Nature Structural Biology.
[15] D. E. Anderson,et al. pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. , 1990, Biochemistry.
[16] S. Gellman. Minimal model systems for β-sheet secondary structure in proteins , 1998 .
[17] M. Jiménez,et al. Thermodynamic Analysis of β-Hairpin-Forming Peptides from the Thermal Dependence of 1H NMR Chemical Shifts , 2002 .
[18] P. Doty,et al. DETERMINATION OF THE PARAMETERS FOR HELIX FORMATION IN POLY-gamma-BENZYL-L-GLUTAMATE. , 1959, Proceedings of the National Academy of Sciences of the United States of America.
[19] B. Zimm,et al. Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains , 1959 .
[20] L. Serrano,et al. De novo design and structural analysis of a model β-hairpin peptide system , 1996, Nature Structural Biology.
[21] R. Bruccoleri,et al. Structural and Dynamic Properties of a .beta.-Hairpin-Forming Linear Peptide. 2. 13C NMR Relaxation Analysis , 1995 .
[22] V. Muñoz,et al. A statistical mechanical model for β-hairpin kinetics , 1998 .
[23] S L Mayo,et al. Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[24] Arto Annila,et al. On the origin of residual dipolar couplings from denatured proteins. , 2003, Journal of the American Chemical Society.
[25] Christopher M. Dobson,et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis , 1997, Nature.
[26] A. Pardi,et al. Hydrogen bond length and proton NMR chemical shifts in proteins , 1983 .
[27] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[28] G. Lipari. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules , 1982 .
[29] M. Searle,et al. Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in Water , 1998 .
[30] J. Thornton,et al. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR , 1996, Journal of biomolecular NMR.
[31] M G Rossmann,et al. Structure of bacteriophage T4 fibritin M: a troublesome packing arrangement. , 1998, Acta crystallographica. Section D, Biological crystallography.
[32] P. V. von Hippel,et al. Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.
[33] J. Sodroski,et al. Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin , 2002, Journal of Virology.
[34] A. Bax,et al. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. , 1998, Journal of magnetic resonance.
[35] R. Hodges,et al. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects , 1995, Journal of biomolecular NMR.
[36] S. Grzesiek,et al. Refined solution structure and backbone dynamics of HIV‐1 Nef , 1997, Protein science : a publication of the Protein Society.
[37] A. Bax,et al. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. , 1997, Science.
[38] D Thirumalai,et al. Mechanisms and kinetics of beta-hairpin formation. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[39] S. Grzesiek,et al. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. , 2004, Journal of molecular biology.
[40] Observation of residual dipolar couplings in short peptides , 2003, Proteins.
[41] L. Serrano,et al. The design of linear peptides that fold as monomeric β-sheet structures , 1999 .
[42] K. Dill,et al. Cooperativity in protein-folding kinetics. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[43] R. Kammerer,et al. Structure and disorder in the ribonuclease S‐peptide probed by NMR residual dipolar couplings , 2003, Protein science : a publication of the Protein Society.
[44] Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor , 1999, Journal of biomolecular NMR.
[45] V. Mesyanzhinov,et al. Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein. , 2002, European Journal of Biochemistry.
[46] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results , 1982 .
[47] W. Wood,et al. Bacteriophage T4 whiskers: a rudimentary environment-sensing device. , 1975, Proceedings of the National Academy of Sciences of the United States of America.
[48] F. Gai,et al. Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin. , 2003, Journal of the American Chemical Society.
[49] S. Grzesiek,et al. Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes , 2000, Journal of biomolecular NMR.
[50] S. Grzesiek,et al. Purple membrane induced alignment of biological macromolecules in the magnetic field , 1999 .
[51] J. Onuchic,et al. Theory of Protein Folding This Review Comes from a Themed Issue on Folding and Binding Edited Basic Concepts Perfect Funnel Landscapes and Common Features of Folding Mechanisms , 2022 .
[52] L. Serrano,et al. Conformational exchange on the microsecond time scale in α-helix and β-hairpin peptides measured by 13C NMR transverse relaxation , 2001 .
[53] R J Fletterick,et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[54] A. Tropsha,et al. Molecular simulations of beta-sheet twisting. , 1996, Journal of molecular biology.
[55] Gerard J A Kroon,et al. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. , 2004, Journal of molecular biology.
[56] D. Baker,et al. Critical role of β-hairpin formation in protein G folding , 2000, Nature Structural Biology.
[57] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[58] V. Muñoz,et al. Folding dynamics and mechanism of β-hairpin formation , 1997, Nature.
[59] S. Lifson,et al. On the Theory of Helix—Coil Transition in Polypeptides , 1961 .
[60] F. Poulsen,et al. Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings. , 2004, Journal of molecular biology.
[61] L. Serrano,et al. A short linear peptide that folds into a native stable β-hairpin in aqueous solution , 1994, Nature Structural Biology.
[62] Y. Ishii,et al. Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole−Dipole Couplings in High-Resolution Biomolecular NMR , 2000 .
[63] David A. Case,et al. Probing multiple effects on 15N, 13Cα, 13Cβ, and 13C′ chemical shifts in peptides using density functional theory , 2002 .
[64] D. Shortle,et al. Robustness of the long-range structure in denatured staphylococcal nuclease to changes in amino acid sequence. , 2002, Biochemistry.
[65] J. Hus,et al. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data , 2000, Journal of biomolecular NMR.
[66] John L Markley,et al. Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange , 2002, Protein science : a publication of the Protein Society.
[67] A. Bax,et al. A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles* , 2001, Journal of biomolecular NMR.
[68] Ad Bax,et al. Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase , 1998 .
[69] S. Griffiths-Jones,et al. Energetics of Weak Interactions in a β-hairpin Peptide: Electrostatic and Hydrophobic Contributions to Stability from Lysine Salt Bridges , 1999 .
[70] A. Bax,et al. Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.
[71] V. Mesyanzhinov,et al. The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin. , 1999, Biochemistry. Biokhimiia.
[72] L Serrano,et al. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. , 1997, Journal of molecular biology.