Pages that link to "Q39200165"

The following pages link to The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor (Q39200165):

Displaying 43 items.

• Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor (Q21045382) ‎ (← links)
• Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures (Q27642124) ‎ (← links)
• Hydrogen exchange and structural dynamics of proteins and nucleic acids (Q28262950) ‎ (← links)
• Hydrogen exchange in BPTI variants that do not share a common disulfide bond (Q30416869) ‎ (← links)
• Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a glycine-to-serine mutation. (Q30417941) ‎ (← links)
• Correlations between internal mobility and stability of globular proteins (Q34251694) ‎ (← links)
• Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design (Q34376818) ‎ (← links)
• A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A (Q36291131) ‎ (← links)
• Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein (Q36592926) ‎ (← links)
• Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor (Q39264985) ‎ (← links)
• Mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor (Q39291846) ‎ (← links)
• 13C-nuclear magnetic resonance-spectral studies of labeled glycophorins. (Q39692782) ‎ (← links)
• Motions in Proteins (Q39856027) ‎ (← links)
• Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor (Q40705813) ‎ (← links)
• The Influence of Localized Chemical Modifications of the Basic Pancreatic Trypsin Inhibitor on Static and Dynamic Aspects of the Molecular Conformation in Solution (Q40715062) ‎ (← links)
• Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys-14 and Cys-38. Influence of Charged Protecting Groups on the Stability of the Protein (Q40715069) ‎ (← links)
• Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor (Q41482987) ‎ (← links)
• N-terminal modification of proteins for fluorescence measurements (Q41487388) ‎ (← links)
• Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor (Q41745237) ‎ (← links)
• Prediction of titration properties of structures of a protein derived from molecular dynamics trajectories (Q41843314) ‎ (← links)
• Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor (Q42064269) ‎ (← links)
• Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A. (Q42842947) ‎ (← links)
• Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins (Q43898083) ‎ (← links)
• A 1H nuclear-magnetic-resonance study of the solution conformation of the isoinhibitor K from Helix pomatia (Q44175998) ‎ (← links)
• Structural Characterization by Nuclear Magnetic Resonance of a Reactive-Site 13Carbon-labelled Basic Pancreatic Trypsin Inhibitor with the Peptide Bond Arg-39-Ala-40 Cleaved and Arg-39 Removed (Q44179483) ‎ (← links)
• pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements (Q44914553) ‎ (← links)
• Contribution of surface salt bridges to protein stability: guidelines for protein engineering (Q48007914) ‎ (← links)
• Improving the accuracy of protein pKa calculations: conformational averaging versus the average structure. (Q52234205) ‎ (← links)
• The contribution of cross‐links to protein stability: A normal mode analysis of the configurational entropy of the native state (Q52407607) ‎ (← links)
• The pH dependence of the equilibrium constant KHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin). (Q52426419) ‎ (← links)
• Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. (Q52590877) ‎ (← links)
• Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution. (Q52659807) ‎ (← links)
• Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. (Q52708432) ‎ (← links)
• Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance (Q57825975) ‎ (← links)
• Dynamic model of globular protein conformations based on NMR studies in solution (Q67381833) ‎ (← links)
• Protein structural fluctuations during a period of 100 ps (Q67471071) ‎ (← links)
• Energetic contribution of solvent-exposed ion pairs to alpha-helix structure (Q67729420) ‎ (← links)
• Characterization of the proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance. Stability, amide proton exchange and mobility of aromatic residues (Q70149880) ‎ (← links)
• A proton-nuclear-magnetic-resonance study at 500 MHz on Megasphaera elsdenii flavodoxin. A study on the stability, proton exchange and the assignment of some resonance lines (Q70201369) ‎ (← links)
• Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor (Q72750352) ‎ (← links)
• Folding pathway of a circular form of bovine pancreatic trypsin inhibitor (Q72753385) ‎ (← links)
• Effect on protein stability of reversing the charge on amino groups (Q72925690) ‎ (← links)
• Solvent accessibility analysis on the mutants of Hsc70 ATPase fragment (Q77337937) ‎ (← links)