Effect of chemical modifications at tryptophan-108 on binding of lanthanide ions to hen egg-white lysozyme. Application of natural-abundance carbon-13 nuclear magnetic resonance spectroscopy

Biochemistry ◽

10.1021/bi00645a010 ◽

1977 ◽

Vol 16 (26) ◽

pp. 5711-5716 ◽

Author(s):

Kilian Dill ◽

Adam Allerhand

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Egg White ◽

Lanthanide Ions ◽

Resonance Spectroscopy ◽

Hen Egg White Lysozyme ◽

Chemical Modifications ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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Participation of tryptophan 62 in the self-association of hen egg white lysozyme. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)40620-x ◽

1977 ◽

Vol 252 (5) ◽

pp. 1795-1798

Author(s):

R S Norton ◽

A Allerhand

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Egg White ◽

The Self ◽

Resonance Spectroscopy ◽

Hen Egg White Lysozyme ◽

Egg White Lysozyme ◽

Hen Egg White ◽

Self Association ◽

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Studies of chemically modified histidine residues of proteins by carbon 13 nuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodoacetate

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)30208-9 ◽

1979 ◽

Vol 254 (7) ◽

pp. 2210-2213

Author(s):

W.J. Goux ◽

A. Allerhand

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Egg White ◽

Resonance Spectroscopy ◽

Hen Egg White Lysozyme ◽

Chemically Modified ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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Studies of individual carbon sites of hen egg white lysozyme by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Assignment of the nonprotonated aromatic carbon resonances to specific residues in the sequence.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)40619-3 ◽

1977 ◽

Vol 252 (5) ◽

pp. 1786-1794 ◽

Author(s):

A Allerhand ◽

R S Norton ◽

R F Childers

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Egg White ◽

Resonance Spectroscopy ◽

Hen Egg White Lysozyme ◽

Aromatic Carbon ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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Studies of chemical modifications of proteins by carbon 13 neuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodine.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)32978-2 ◽

1976 ◽

Vol 251 (21) ◽

pp. 6522-6528

Author(s):

R S Norton ◽

A Allerhand

Keyword(s):

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Egg White ◽

Resonance Spectroscopy ◽

Hen Egg White Lysozyme ◽

Chemical Modifications ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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An analysis of the cobalt(2+) ion-induced nuclear magnetic resonance perturbations of hen egg white lysozyme

Biochemistry ◽

10.1021/bi00601a016 ◽

1978 ◽

Vol 17 (8) ◽

pp. 1463-1468 ◽

Author(s):

R. E. Lenkinski ◽

D. G. Agresti ◽

D. M. Chen ◽

J. D. Glickson

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Egg White ◽

Hen Egg White Lysozyme ◽

Egg White Lysozyme ◽

Hen Egg White ◽

Hen Egg ◽

Nuclear Magnetic

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Self-association of hen egg-white lysozyme as studied by nuclear magnetic resonance

Biochemistry ◽

10.1021/bi00636a025 ◽

1977 ◽

Vol 16 (17) ◽

pp. 3879-3882 ◽

Author(s):

Heisaburo Shindo ◽

Jack S. Cohen ◽

John A. Rupley

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Egg White ◽

Hen Egg White Lysozyme ◽

Egg White Lysozyme ◽

Hen Egg White ◽

Self Association ◽

Hen Egg ◽

Nuclear Magnetic

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Hen egg white lysozyme: carbon-13 nuclear magnetic resonance assignments and dependence of conformational flexibility on inhibitor binding and temperature

Biochemistry ◽

10.1021/bi00310a021 ◽

1984 ◽

Vol 23 (15) ◽

pp. 3522-3526 ◽

Author(s):

Oliver W. Howarth ◽

L. Yun Lian

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Resonance Assignments ◽

Egg White ◽

Conformational Flexibility ◽

Hen Egg White Lysozyme ◽

Inhibitor Binding ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. II. Spectral assignments and inhibitor binding in hen egg-white lysozyme.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.60.1.92 ◽

1968 ◽

Vol 60 (1) ◽

pp. 92-99 ◽

Author(s):

J. S. Cohen ◽

O. Jardetzky

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Binding Sites ◽

Egg White ◽

Hen Egg White Lysozyme ◽

Inhibitor Binding ◽

Magnetic Resonance Studies ◽

Egg White Lysozyme ◽

Hen Egg White ◽

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Pressure-assisted cold denaturation of hen egg white lysozyme: the influence of co-solvents probed by hydrogen exchange nuclear magnetic resonance

Brazilian Journal of Medical and Biological Research ◽

10.1590/s0100-879x2005000800005 ◽

2005 ◽

Vol 38 (8) ◽

pp. 1185-1193 ◽

Author(s):

K. Vogtt ◽

R. Winter

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Hydrogen Exchange ◽

Egg White ◽

Hen Egg White Lysozyme ◽

Cold Denaturation ◽

Egg White Lysozyme ◽

Hen Egg White ◽

Hen Egg ◽

Nuclear Magnetic

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Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.73.6.1979 ◽

1976 ◽

Vol 73 (6) ◽

pp. 1979-1983 ◽

Author(s):

H. Shindo ◽

J. S. Cohen

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Egg White ◽

Carboxyl Groups ◽

Hen Egg White Lysozyme ◽

Egg White Lysozyme ◽

13C Nuclear Magnetic Resonance ◽

Hen Egg White ◽

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