Probing the conformational state of apomyoglobin by limited proteolysis 1 1 Edited by P. E. Wright
Angelo Fontana
Journal of Molecular Biology, 1997
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Structural Characterization of the Molten Globule State of Apomyoglobin by Limited Proteolysis and HPLC-Mass Spectrometry †
Young Kim
Biochemistry, 2005
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Nicked Apomyoglobin: A Noncovalent Complex of Two Polypeptide Fragments Comprising the Entire Protein Chain †
Vincenzo Filippis
Biochemistry, 2004
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Probing protein structure by limited proteolysis
Angelo Fontana
2004
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Unfolding pathway of myoglobin: Molecular properties of intermediate forms
Giovanni Colonna, Gaetano Irace
Archives of Biochemistry and Biophysics, 1986
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Conformational substates and motions in myoglobin. External influences on structure and dynamics
P. Ormos
Biophysical Journal, 1990
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Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K
H. Frauenfelder
Proceedings of the National Academy of Sciences, 1982
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Circular Permutation and Deletion Studies of Myoglobin Indicate that the Correct Position of Its N-Terminus Is Required for Native Stability and Solubility but Not for Native-like Heme Binding and Folding †
Carlos Arias Ramos
Biochemistry, 2005
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Folding propensities of peptide fragments of myoglobin
Gene merutka
Protein Science, 2008
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Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements
Alessandro Negro
Protein Science, 2004
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Immunological measurements of conformational motility in regions of the myoglobin molecule
John Hurrell
Biochemistry, 1977
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Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobin
Gene merutka
Biochemistry, 1993
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Protein tertiary structure and the myoglobin phase diagram
Alexander Molochkov
Scientific Reports
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On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding
Vitaly Melnik
Molecular Biology, 2009
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The effect of tryptophanyl substitution on folding and structure of myoglobin
rita casadio
European Journal of Biochemistry, 2000
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Protein engineering studies of myoglobin
Robert Maurus
1998
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Stability of Myoglobin: A Model for the Folding of Heme Proteins
Szymon Krzywda
Biochemistry, 1994
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The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent
Yuji O Kamatari
Protein Science, 2008
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A Comparative NMR Study of the Polypeptide Backbone Dynamics of Hemoglobin in the Deoxy and Carbonmonoxy Forms
sarata sahu
Biochemistry, 2007
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Equilibrium folding-unfolding pathways of model proteins: Effect of myoglobin-heme contacts
Robert Jernigan
Biopolymers, 1983
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Structure of prothrombin in the closed form reveals new details on the mechanism of activation
Leslie Pelc
Scientific reports, 2018
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Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography
Alessandro Arcovito
Proceedings of the National Academy of Sciences, 2006
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A Circularly Permuted Myoglobin Possesses a Folded Structure and Ligand Binding Similar to Those of the Wild-Type Protein but with a Reduced Thermodynamic Stability †
David Peyton
Biochemistry, 2002
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Evidence of an associative intermediate on the myoglobin refolding pathway
Hiroshi Kihara
Biophysical Journal, 1993
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Kinetic Intermediates of Holo- and Apo-Myoglobin Studied Using HDX-TIMS-MS and Molecular Dynamic Simulations
Jaroslava Miksovska
Journal of The American Society for Mass Spectrometry, 2015
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Conformational substates in enzyme mechanism: The 120 K structure of α-lytic protease at 1.5 Å resolution
David Agard
Protein Science, 1997
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Modeling of Ligation-Induced Helix/Loop Displacements in Myoglobin: Toward an Understanding of Hemoglobin Allostery
Andrzej Jarzęcki
Journal of the American Chemical Society, 2006
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Computer simulations of apomyoglobin folding
Mariangela Dametto
2009
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A low resolution model of fragment 1 from bovine prothrombin
Oliver Lindqvist
FEBS Letters, 1982
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A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket
Christopher Overall
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
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Conformational stability of neuroglobin helix F - possible effects on the folding pathway within the globin family
Gennaro Esposito
FEBS Journal, 2009
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Dynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein
E. Fabiani
European Biophysics Journal, 2009
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