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Refinado por: data de publicação: 1979Até1993 remover
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1
Protein Structure Comparison by Alignment of Distance Matrices
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Protein Structure Comparison by Alignment of Distance Matrices

Holm, Liisa ; Sander, Chris

Journal of molecular biology, 1993-09, Vol.233 (1), p.123-138 [Periódico revisado por pares]

Oxford: Elsevier Ltd

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THE FOLDING OF HEN LYSOZYME INVOLVES PARTIALLY STRUCTURED INTERMEDIATES AND MULTIPLE PATHWAYS
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THE FOLDING OF HEN LYSOZYME INVOLVES PARTIALLY STRUCTURED INTERMEDIATES AND MULTIPLE PATHWAYS

RADFORD, SE ; DOBSON, CM ; EVANS, PA

Nature (London), 1992-07, Vol.358 (6384), p.302-307 [Periódico revisado por pares]

LONDON: MACMILLAN MAGAZINES LTD

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3
Human lysozyme gene mutations cause hereditary systemic amyloidosis
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Human lysozyme gene mutations cause hereditary systemic amyloidosis

Pepys, M B ; Hawkins, P N ; Booth, D R ; Vigushin, D M ; Tennent, G A ; Soutar, A K ; Totty, N ; Nguyen, O ; Blake, C C ; Terry, C J

Nature (London), 1993-04, Vol.362 (6420), p.553-557 [Periódico revisado por pares]

England: Nature Publishing Group

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4
Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds
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Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds

Wade, Rebecca C. ; Goodford, Peter J.

Journal of medicinal chemistry, 1993, Vol.36 (1), p.148-156 [Periódico revisado por pares]

United States: American Chemical Society

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5
Response of a Protein Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic Effect
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Response of a Protein Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic Effect

Eriksson, A. E. ; Baase, W. A. ; X.-J. Zhang ; Heinz, D. W. ; Blaber, M. ; Baldwin, E. P. ; Matthews, B. W.

Science (American Association for the Advancement of Science), 1992-01, Vol.255 (5041), p.178-183 [Periódico revisado por pares]

WASHINGTON: American Society for the Advancement of Science

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6
Contribution of Hydration to Protein Folding Thermodynamics: I. The Enthalpy of Hydration
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Contribution of Hydration to Protein Folding Thermodynamics: I. The Enthalpy of Hydration

Makhatadze, George I. ; Privalov, Peter L.

Journal of molecular biology, 1993-07, Vol.232 (2), p.639-659 [Periódico revisado por pares]

Oxford: Elsevier Ltd

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7
Protein interactions with urea and guanidinium chloride: A calorimetric study
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Protein interactions with urea and guanidinium chloride: A calorimetric study

Makhatadze, George I. ; Privalov, Peter L.

Journal of molecular biology, 1992-07, Vol.226 (2), p.491-505 [Periódico revisado por pares]

LONDON: Elsevier Ltd

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8
Detection of Transient Protein Folding Populations by Mass Spectrometry
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Detection of Transient Protein Folding Populations by Mass Spectrometry

Miranker, Andrew ; Robinson, Carol V. ; Radford, Sheena E. ; Aplin, Robin T. ; Dobson, Christopher M.

Science (American Association for the Advancement of Science), 1993-11, Vol.262 (5135), p.896-900 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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9
Contribution of Hydration to Protein Folding Thermodynamics: II. The Entropy and Gibbs Energy of Hydration
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Contribution of Hydration to Protein Folding Thermodynamics: II. The Entropy and Gibbs Energy of Hydration

Privalov, Peter L. ; Makhatadze, George I.

Journal of molecular biology, 1993-07, Vol.232 (2), p.660-679 [Periódico revisado por pares]

Oxford: Elsevier Ltd

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10
Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation
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Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation

HUGGINS, T. G ; WELLS-KNECHT, M. C ; DETORIE, N. A ; BAYNES, J. W ; THORPE, S. R

The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12341-12347 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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