Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein.
about
Physicochemical Properties of Ion Pairs of Biological MacromoleculesA Virtual Mixture Approach to the Study of Multistate Equilibrium: Application to Constant pH Simulation in Explicit WaterAccommodation of a central arginine in a transmembrane peptide by changing the placement of anchor residues.Dynamic Equilibria of Short-Range Electrostatic Interactions at Molecular Interfaces of Protein-DNA Complexes.Observing in-phase single-quantum 15N multiplets for NH2/NH3+ groups with two-dimensional heteronuclear correlation spectroscopy.Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH.Myristate exposure in the human immunodeficiency virus type 1 matrix protein is modulated by pH.Progress in the prediction of pKa values in proteinsStructural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.Rapid calculation of protein pKa values using Rosetta.Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopyDifferences in lysine pKa values may be used to improve NMR signal dispersion in reductively methylated proteins.The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.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.Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy.Microscopic mechanisms that govern the titration response and pKa values of buried residues in staphylococcal nuclease mutants.MCCE analysis of the pKas of introduced buried acids and bases in staphylococcal nuclease.
P2860
Q26782002-4532F6FC-C95E-468A-9C4B-F09CEFC1D863Q28550522-D5734310-E809-4EB4-BC3E-15EB6C3B3ECCQ30571704-9955F6A9-9FB2-41FE-A92C-A7815F82D0CAQ30982412-D65D7517-05B0-4634-97E2-AB2FB48440D9Q33359039-3D038477-792F-476B-8193-60E1BDEF1883Q33449219-7CA08895-D59A-45F5-9DB2-FE1708F00A1DQ34544143-34F8BE6D-0F07-4706-9B89-61FDACF011ACQ35627466-4B2EDFB3-57A8-4D34-BD78-00C68F3F803DQ36026100-C8BD1124-4E13-4F2A-B9E8-F9D945C4BC06Q36150734-F4BF7B79-D947-41E0-9167-B57DC2CC74C9Q37040440-F42A3A50-23A8-46E3-B6B5-5175E910C517Q41998268-02EDE386-CE5E-4DDB-BF60-D2D56D5CCC5AQ42603124-D972F691-0331-4BD0-B858-BDADA732CDC9Q44914553-C199C675-3096-483D-A610-FD1962FA3D60Q48191212-CECAE116-F95A-42CC-A682-6E766F09FAFAQ51318577-2BDB3DDF-4547-4D7D-A974-629CB9F079E7Q51532804-E7846EB9-1BFB-4208-BDAB-A991944C0B14
P2860
Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein.
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@ast
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@en
type
label
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@ast
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@en
prefLabel
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@ast
Direct evidence for deprotonat ...... hydrophobic core of a protein.
@en
P2093
P356
P1476
Direct evidence for deprotonat ...... hydrophobic core of a protein
@en
P2093
Bertrand García-Moreno
Carlos A Castañeda
Michael Chimenti
Yuki Takayama
P304
P356
10.1021/JA801731G
P407
P577
2008-05-03T00:00:00Z