Mapping the Conformational Stability of Maltose Binding Protein at the Residue Scale Using Nuclear Magnetic Resonance Hydrogen Exchange Experiments

Magnetic Resonance ◽

Hydrogen Exchange ◽

Binding Protein ◽

Conformational Stability ◽

Maltose Binding Protein ◽

Methods in Enzymology - Nuclear Magnetic Resonance of Biological Macromolecules - Part B ◽

Nuclear Magnetic Resonance Methods for High Molecular Weight Proteins: A Study Involving a Complex of Maltose Binding Protein and β-Cyclodextrin

10.1016/s0076-6879(01)39314-x ◽

2001 ◽

pp. 174-203 ◽

Cited By ~ 18

Author(s):

Lewis E. Kay

Keyword(s):

Molecular Weight ◽

Magnetic Resonance ◽

High Molecular Weight ◽

Binding Protein ◽

Maltose Binding Protein ◽

High Molecular Weight Proteins ◽

Proton nuclear magnetic resonance spectroscopy and ligand binding dynamics of the Escherichia coli L-arabinose binding protein

Biochemistry ◽

10.1021/bi00538a035 ◽

1982 ◽

Vol 21 (9) ◽

pp. 2227-2233 ◽

Cited By ~ 15

Author(s):

Abbot F. Clark ◽

Thomas A. Gerken ◽

Robert W. Hogg

Keyword(s):

Escherichia Coli ◽

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Ligand Binding ◽

Nuclear Magnetic Resonance Spectroscopy ◽

Binding Protein ◽

Proton Nuclear Magnetic Resonance ◽

Resonance Spectroscopy ◽

A proton nuclear magnetic resonance investigation of histine-binding protein J of salmonella typhimurium: A model for transport of L-histidine across cytoplasmic membrane

Journal of Supramolecular Structure ◽

10.1002/jss.400130202 ◽

1980 ◽

Vol 13 (2) ◽

pp. 131-145 ◽

Cited By ~ 8

Author(s):

Chien Ho ◽

Yueh-hua Giza ◽

Seizo Takahashi ◽

Kenneth E. Ugen ◽

Patricia F. Cottam ◽

...

Keyword(s):

Magnetic Resonance ◽

Salmonella Typhimurium ◽

Cytoplasmic Membrane ◽

Binding Protein ◽

Proton Nuclear Magnetic Resonance ◽

Resonance Investigation ◽

Nuclear Magnetic Resonance Investigation ◽

Magnetic Resonance Investigation ◽

Population and Structure Determination of Hidden Folding Intermediates by Native-State Hydrogen Exchange-Directed Protein Engineering and Nuclear Magnetic Resonance

Protein Folding Protocols ◽

10.1385/1-59745-189-4:69 ◽

2006 ◽

pp. 69-82

Author(s):

Yawen Bai ◽

Hanqiao Feng ◽

Zheng Zhou

Keyword(s):

Magnetic Resonance ◽

Protein Engineering ◽

Structure Determination ◽

Hydrogen Exchange ◽

Native State ◽

Folding Intermediates ◽

Conformation of a Trimannoside Bound to Mannose-Binding Protein by Nuclear Magnetic Resonance and Molecular Dynamics Simulations

Biophysical Journal ◽

10.1016/s0006-3495(02)75610-5 ◽

2002 ◽

Vol 82 (5) ◽

pp. 2683-2699 ◽

Cited By ~ 16

Author(s):

Eric W. Sayers ◽

James H. Prestegard

Keyword(s):

Molecular Dynamics ◽

Magnetic Resonance ◽

Molecular Dynamics Simulations ◽

Binding Protein ◽

Mannose Binding Protein ◽

Mannose Binding ◽

Dynamics Simulations ◽

Site-Specific Free Energy Changes in Proteins upon Ligand Binding by Nuclear Magnetic Resonance: Ca2+-Displacement by Ln3+ in a Ca2+-Binding Protein from Entamoeba histolytica

Chemical Biology & Drug Design ◽

10.1111/j.1747-0285.2011.01090.x ◽

2011 ◽

Vol 77 (4) ◽

pp. 272-280

Author(s):

Kousik Chandra ◽

Sourajit M. Mustafi ◽

Subramanian Muthukumar ◽

Kandala V. R. Chary

Keyword(s):

Free Energy ◽

Magnetic Resonance ◽

Ligand Binding ◽

Entamoeba Histolytica ◽

Binding Protein ◽

Site Specific ◽

Specific Free Energy ◽

Hydrogen exchange in the hydrophilic regions of detergent-solubilized M13 coat protein detected by 13C nuclear magnetic resonance isotope shifts

Biophysical Journal ◽

10.1016/s0006-3495(86)83645-1 ◽

1986 ◽

Vol 49 (1) ◽

pp. 329-331 ◽

Cited By ~ 15

Author(s):

G.D. Henry ◽

J.D. O'Neil ◽

J.H. Weiner ◽

B.D. Sykes

Keyword(s):

Magnetic Resonance ◽

Coat Protein ◽

Hydrogen Exchange ◽

Isotope Shifts ◽

13C Nuclear Magnetic Resonance ◽

Molecular genetic, biochemical and nuclear magnetic resonance studies on the role of the tryptophan residues of glutamine-binding protein from Escherichia coli

Journal of Molecular Biology ◽

10.1016/0022-2836(89)90113-7 ◽

1989 ◽

Vol 210 (4) ◽

pp. 859-867 ◽

Cited By ~ 8

Author(s):

Qichang Shen ◽

Virgil Simplaceanu ◽

Patricia F. Cottam ◽

Jing-Lun Wu ◽

Jen-Shiang Hong ◽

...

Keyword(s):

Escherichia Coli ◽

Magnetic Resonance ◽

Binding Protein ◽

Molecular Genetic ◽

Magnetic Resonance Studies ◽

Tryptophan Residues ◽

Hydrogen Exchange of Individual Amide Protons in the E. ColilacRepressor DNA-binding Domain: A Nuclear Magnetic Resonance Study (29)

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.1985.10508416 ◽

1985 ◽

Vol 3 (2) ◽

pp. 269-280 ◽

Cited By ~ 14

Author(s):

R. Boelens ◽

P. Gros ◽

R. M. Scheek ◽

J. A. Verpoorte ◽

R. Kaptein

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Hydrogen Exchange ◽

Nuclear Magnetic Resonance Study ◽

Binding Domain ◽

Dna Binding Domain ◽

Magnetic Resonance Study ◽

Nuclear Magnetic ◽

Amide Protons

A nuclear magnetic resonance study of the hydrogen-exchange behaviour of lysozyme in crystals and solution

Journal of Molecular Biology ◽

10.1016/0022-2836(91)90722-i ◽

1991 ◽

Vol 218 (2) ◽

pp. 413-426 ◽

Cited By ~ 67

Author(s):

Torben Graves Pedersen ◽

Bent W. Sigurskjold ◽

Kim V. Andersen ◽

Mogens Kjær ◽

Flemming M. Poulsen ◽

...

Keyword(s):

Magnetic Resonance ◽

Hydrogen Exchange ◽

Nuclear Magnetic Resonance Study ◽

Magnetic Resonance Study ◽

Exchange Behaviour ◽