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Refinado por: Nome da Publicação: Biochemistry remover assunto: Hydrogen-Ion Concentration remover Chemical Phenomena remover
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1
Mucoadhesive polyelectrolyte microparticles containing recombinant human insulin and its analogs aspart and lispro
Mucoadhesive polyelectrolyte microparticles containing recombinant human insulin and its analogs aspart and lispro
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Mucoadhesive polyelectrolyte microparticles containing recombinant human insulin and its analogs aspart and lispro

Balabushevich, N. G. ; Pechenkin, M. A. ; Zorov, I. N. ; Shibanova, E. D. ; Larionova, N. I.

Biochemistry (Moscow), 2011-03, Vol.76 (3), p.327-331 [Periódico revisado por pares]

Dordrecht: SP MAIK Nauka/Interperiodica

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2
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

Wishart, D. S ; Sykes, B. D ; Richards, F. M

Biochemistry (Easton), 1992-02, Vol.31 (6), p.1647-1651 [Periódico revisado por pares]

WASHINGTON: American Chemical Society

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3
Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin
Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin
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Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin

Li, Tiansheng ; Quillin, Michael L ; Phillips, George N ; Olson, John S

Biochemistry (Easton), 1994-02, Vol.33 (6), p.1433-1446 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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4
Direct Force Measurements of Specific and Nonspecific Protein Interactions
Direct Force Measurements of Specific and Nonspecific Protein Interactions
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Direct Force Measurements of Specific and Nonspecific Protein Interactions

Leckband, D. E ; Schmitt, F.-J ; Israelachvili, J. N ; Knoll, W

Biochemistry (Easton), 1994-04, Vol.33 (15), p.4611-4624 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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5
Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
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Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility

Tamura, Youjiro ; Gekko, Kunihiko

Biochemistry (Easton), 1995-02, Vol.34 (6), p.1878-1884 [Periódico revisado por pares]

United States: American Chemical Society

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6
The Substrate Binding Site of Human Liver Cytochrome P450 2C9: An Approach Using Designed Tienilic Acid Derivatives and Molecular Modeling
The Substrate Binding Site of Human Liver Cytochrome P450 2C9: An Approach Using Designed Tienilic Acid Derivatives and Molecular Modeling
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The Substrate Binding Site of Human Liver Cytochrome P450 2C9: An Approach Using Designed Tienilic Acid Derivatives and Molecular Modeling

Mancy, Annah ; Broto, Pierre ; Dijols, Sylvie ; Dansette, Patrick M ; Mansuy, Daniel

Biochemistry (Easton), 1995-08, Vol.34 (33), p.10365-10375 [Periódico revisado por pares]

United States: American Chemical Society

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7
Potassium monopersulfate and a water-soluble manganese porphyrin complex, [Mn(TMPyP)](OAc)5, as an efficient reagent for the oxidative cleavage of DNA
Potassium monopersulfate and a water-soluble manganese porphyrin complex, [Mn(TMPyP)](OAc)5, as an efficient reagent for the oxidative cleavage of DNA
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Potassium monopersulfate and a water-soluble manganese porphyrin complex, [Mn(TMPyP)](OAc)5, as an efficient reagent for the oxidative cleavage of DNA

Bernadou, Jean ; Pratviel, Genevieve ; Bennis, Faiza ; Girardet, Marc ; Meunier, Bernard

Biochemistry (Easton), 1989-09, Vol.28 (18), p.7268-7275 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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8
Interaction of Escherichia coli Cobalamin-Dependent Methionine Synthase and Its Physiological Partner Flavodoxin:  Binding of Flavodoxin Leads to Axial Ligand Dissociation from the Cobalamin Cofactor
Interaction of Escherichia coli Cobalamin-Dependent Methionine Synthase and Its Physiological Partner Flavodoxin:  Binding of Flavodoxin Leads to Axial Ligand Dissociation from the Cobalamin Cofactor
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Interaction of Escherichia coli Cobalamin-Dependent Methionine Synthase and Its Physiological Partner Flavodoxin:  Binding of Flavodoxin Leads to Axial Ligand Dissociation from the Cobalamin Cofactor

Hoover, David M ; Jarrett, Joseph T ; Sands, Richard H ; Dunham, William R ; Ludwig, Martha L ; Matthews, Rowena G

Biochemistry (Easton), 1997-01, Vol.36 (1), p.127-138 [Periódico revisado por pares]

United States: American Chemical Society

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9
A pre-transition-state mimic of an enzyme: x-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
A pre-transition-state mimic of an enzyme: x-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
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A pre-transition-state mimic of an enzyme: x-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water

Wilson, David K ; Quiocho, Florante A

Biochemistry (Easton), 1993-02, Vol.32 (7), p.1689-1694 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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10
Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition
Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition
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Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition

Blankenburg, R ; Meller, P ; Ringsdorf, H ; Salesse, C

Biochemistry (Easton), 1989-10, Vol.28 (20), p.8214-8221 [Periódico revisado por pares]

United States: American Chemical Society

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