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Refinado por: Nome da Publicação: Biochemistry remover assunto: Thermodynamics remover
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1
Hydrogen Bonds: Simple after All?
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Hydrogen Bonds: Simple after All?

Herschlag, Daniel ; Pinney, Margaux M

Biochemistry (Easton), 2018-06, Vol.57 (24), p.3338-3352 [Periódico revisado por pares]

United States: American Chemical Society

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2
Conformational Stability Adaptation of a Double-Stranded RNA-Binding Domain to Transfer RNA Ligand
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Conformational Stability Adaptation of a Double-Stranded RNA-Binding Domain to Transfer RNA Ligand

Bou-Nader, Charles ; Pecqueur, Ludovic ; Barraud, Pierre ; Fontecave, Marc ; Tisné, Carine ; Sacquin-Mora, Sophie ; Hamdane, Djemel

Biochemistry (Easton), 2019-05, Vol.58 (20), p.2463-2473 [Periódico revisado por pares]

United States: American Chemical Society

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3
Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions
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Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions

Martin, Erik W ; Mittag, Tanja

Biochemistry (Easton), 2018-05, Vol.57 (17), p.2478-2487 [Periódico revisado por pares]

United States: American Chemical Society

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4
On the Temperature Dependence of Enzyme-Catalyzed Rates
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On the Temperature Dependence of Enzyme-Catalyzed Rates

Arcus, Vickery L ; Prentice, Erica J ; Hobbs, Joanne K ; Mulholland, Adrian J ; Van der Kamp, Marc W ; Pudney, Christopher R ; Parker, Emily J ; Schipper, Louis A

Biochemistry (Easton), 2016-03, Vol.55 (12), p.1681-1688 [Periódico revisado por pares]

United States: American Chemical Society

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5
A β‑Turn Motif in the Steroid Hormone Receptor’s Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52
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A β‑Turn Motif in the Steroid Hormone Receptor’s Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52

Byrne, Cillian ; Henen, Morkos A ; Belnou, Mathilde ; Cantrelle, François-Xavier ; Kamah, Amina ; Qi, Haoling ; Giustiniani, Julien ; Chambraud, Béatrice ; Baulieu, Etienne-Emile ; Lippens, Guy ; Landrieu, Isabelle ; Jacquot, Yves

Biochemistry (Easton), 2016-09, Vol.55 (38), p.5366-5376 [Periódico revisado por pares]

United States: American Chemical Society

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6
Unexpected Effects of Macromolecular Crowding on Protein Stability
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Unexpected Effects of Macromolecular Crowding on Protein Stability

Benton, Laura A ; Smith, Austin E ; Young, Gregory B ; Pielak, Gary J

Biochemistry (Easton), 2012-12, Vol.51 (49), p.9773-9775 [Periódico revisado por pares]

United States: American Chemical Society

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7
Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV‑2 nsp3
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Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV‑2 nsp3

Frick, David N ; Virdi, Rajdeep S ; Vuksanovic, Nemanja ; Dahal, Narayan ; Silvaggi, Nicholas R

Biochemistry (Easton), 2020-07, Vol.59 (28), p.2608-2615 [Periódico revisado por pares]

United States: American Chemical Society

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8
On the Charge Regulation of Proteins
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On the Charge Regulation of Proteins

Lund, Mikael ; Jönsson, Bo

Biochemistry (Easton), 2005-04, Vol.44 (15), p.5722-5727 [Periódico revisado por pares]

United States: American Chemical Society

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9
Effect of Molecular Crowding on the Stability of RNA G‑Quadruplexes with Various Numbers of Quartets and Lengths of Loops
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Effect of Molecular Crowding on the Stability of RNA G‑Quadruplexes with Various Numbers of Quartets and Lengths of Loops

Matsumoto, Saki ; Tateishi-Karimata, Hisae ; Takahashi, Shuntaro ; Ohyama, Tatsuya ; Sugimoto, Naoki

Biochemistry (Easton), 2020-07, Vol.59 (28), p.2640-2649 [Periódico revisado por pares]

United States: American Chemical Society

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10
Increasing Enzyme Stability and Activity through Hydrogen Bond-Enhanced Halogen Bonds
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Increasing Enzyme Stability and Activity through Hydrogen Bond-Enhanced Halogen Bonds

Carlsson, Anna-Carin C ; Scholfield, Matthew R ; Rowe, Rhianon K ; Ford, Melissa Coates ; Alexander, Austin T ; Mehl, Ryan A ; Ho, P. Shing

Biochemistry (Easton), 2018-07, Vol.57 (28), p.4135-4147 [Periódico revisado por pares]

United States: American Chemical Society

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