UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

Cavities determine the pressure unfolding of proteins

Proceedings of the National Academy of Sciences - PNAS, 2012-05, Vol.109 (18), p.6945-6950

2012

Volltextzugriff (PDF)

Arginine residues at internal positions in a protein are always charged

Proceedings of the National Academy of Sciences - PNAS, 2011-11, Vol.108 (47), p.18954-18959

2011

Volltextzugriff (PDF)

Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii

Biochimica et biophysica acta. General subjects, 2018-12, Vol.1862 (12), p.2660-2673

2018

Volltextzugriff (PDF)

Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein

Proceedings of the National Academy of Sciences - PNAS, 2014-08, Vol.111 (32), p.11685-11690

2014

Volltextzugriff (PDF)

Structural Reorganization Triggered by Charging of Lys Residues in the Hydrophobic Interior of a Protein

Structure (London), 2012-06, Vol.20 (6), p.1071-1085

2012

Volltextzugriff (PDF)

Redox control of iodotyrosine deiodinase

Protein science, 2019-01, Vol.28 (1), p.68-78

2019

Volltextzugriff (PDF)

Electrostatic Effects in a Network of Polar and Ionizable Groups in Staphylococcal Nuclease

Journal of molecular biology, 2008-06, Vol.379 (5), p.1045-1062

2008

Volltextzugriff (PDF)

Heme d formation in a Shewanella benthica hemoglobin

Journal of inorganic biochemistry, 2024-10, Vol.259, p.112654, Article 112654

2024

Volltextzugriff (PDF)

Role of Flexibility and Polarity as Determinants of the Hydration of Internal Cavities and Pockets in Proteins

Biophysical journal, 2007-10, Vol.93 (8), p.2791-2804

2007

Volltextzugriff (PDF)

Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change?

Biophysical journal, 2004-12, Vol.87 (6), p.3982-3994

2004

Volltextzugriff (PDF)

Dielectric Properties of a Protein Probed by Reversal of a Buried Ion Pair

The journal of physical chemistry. B, 2018-03, Vol.122 (9), p.2516-2524

2018

Volltextzugriff (PDF)

Control of distal lysine coordination in a monomeric hemoglobin: A role for heme peripheral interactions

Journal of inorganic biochemistry, 2021-06, Vol.219, p.111437, Article 111437

2021

Volltextzugriff (PDF)

Charges in Hydrophobic Environments: A Strategy for Identifying Alternative States in Proteins

Biochemistry (Easton), 2017-01, Vol.56 (1), p.212-218

2017

Volltextzugriff (PDF)

Local Backbone Flexibility as a Determinant of the Apparent pKa Values of Buried Ionizable Groups in Proteins

Biochemistry (Easton), 2017-10, Vol.56 (40), p.5338-5346

2017

Volltextzugriff (PDF)

The pK(a) values of acidic and basic residues buried at the same internal location in a protein are governed by different factors

Journal of molecular biology, 2009-05, Vol.389 (1), p.34

2009

Volltextzugriff (PDF)

Local Backbone Flexibility as a Determinant of the Apparent pK a Values of Buried Ionizable Groups in Proteins

Biochemistry (Easton), 2017-10, Vol.56 (40), p.5338-5346

2017

Volltextzugriff (PDF)

Anomalous Properties of Lys Residues Buried in the Hydrophobic Interior of a Protein Revealed with 15 N-Detect NMR Spectroscopy

The journal of physical chemistry letters, 2018-01, Vol.9 (2), p.383-387

2018

Volltextzugriff (PDF)

Molecular determinants of the pKa values of Asp and Glu residues in staphylococcal nuclease

Proteins, structure, function, and bioinformatics, 2009-11, Vol.77 (3), p.570-588

2009

Volltextzugriff (PDF)

The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures

Proteins, structure, function, and bioinformatics, 2014-03, Vol.82 (3), p.528-534

2014

Volltextzugriff (PDF)

A buried lysine that titrates with a normal pKa: role of conformational flexibility at the protein-water interface as a determinant of pKa values

Protein science, 2008-05, Vol.17 (5), p.833

2008

Volltextzugriff (PDF)

Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation

Acta crystallographica. Section F, Structural biology and crystallization communications, 2015-06, Vol.71 (6), p.718-725

2015

Volltextzugriff (PDF)

Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups

Biophysical journal, 2008-04, Vol.94 (8), p.3208-3216

2008

Volltextzugriff (PDF)

Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum

Journal of molecular biology, 1998-07, Vol.280 (4), p.669-685

1998

Volltextzugriff (PDF)

Charges in hydrophobic environments in proteins: A study of arginine ion-pairs

Biophysical journal, 2024-02, Vol.123 (3), p.555a-555a

2024

Volltextzugriff (PDF)

Ion Pairs Buried in Hydrophobic Environments within Proteins: Electrostatic Crosstalk between Buried Groups

Biophysical journal, 2019-02, Vol.116 (3), p.187a-187a

2019

Volltextzugriff (PDF)

1 – 25 von 64

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(60)
Mit Volltextzugriff
(62)

Publikationsform

Artikel
(63)
Tagungsberichte
(1)

Sprache

Englisch
(64)

Erscheinungsjahr

n.n

Menü

Weitere Dienste

Einstellungen

Cavities determine the pressure unfolding of proteins

Arginine residues at internal positions in a protein are always charged

Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii

Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein

Structural Reorganization Triggered by Charging of Lys Residues in the Hydrophobic Interior of a Protein

Redox control of iodotyrosine deiodinase

Electrostatic Effects in a Network of Polar and Ionizable Groups in Staphylococcal Nuclease

Heme d formation in a Shewanella benthica hemoglobin

Role of Flexibility and Polarity as Determinants of the Hydration of Internal Cavities and Pockets in Proteins

Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change?

Dielectric Properties of a Protein Probed by Reversal of a Buried Ion Pair

Control of distal lysine coordination in a monomeric hemoglobin: A role for heme peripheral interactions

Charges in Hydrophobic Environments: A Strategy for Identifying Alternative States in Proteins

Local Backbone Flexibility as a Determinant of the Apparent pKa Values of Buried Ionizable Groups in Proteins

The pK(a) values of acidic and basic residues buried at the same internal location in a protein are governed by different factors

Local Backbone Flexibility as a Determinant of the Apparent pK a Values of Buried Ionizable Groups in Proteins

Anomalous Properties of Lys Residues Buried in the Hydrophobic Interior of a Protein Revealed with 15 N-Detect NMR Spectroscopy

Molecular determinants of the pKa values of Asp and Glu residues in staphylococcal nuclease

The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures

A buried lysine that titrates with a normal pKa: role of conformational flexibility at the protein-water interface as a determinant of pKa values

Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation

Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups

Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum

Charges in hydrophobic environments in proteins: A study of arginine ion-pairs

Ion Pairs Buried in Hydrophobic Environments within Proteins: Electrostatic Crosstalk between Buried Groups

Suchergebnisse filtern