Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy
about
Are the parameters of various stabilization factors estimated from mutant human lysozymes compatible with other proteins?Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in waterHydrogen bonding stabilizes globular proteins.Identification of a site in the phosphocarrier protein, HPr, which influences its interactions with sugar permeases of the bacterial phosphotransferase system: kinetic analyses employing site-specific mutants.Equilibrium constants and free energies in unfolding of proteins in urea solutionsMass spectrometric measurement of changes in protein hydrogen exchange rates that result from point mutations.
P2860
Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@en
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@nl
type
label
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@en
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@nl
prefLabel
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@en
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@nl
P2093
P2860
P356
P1433
P1476
Investigation of a side-chain- ...... dynamics, and NMR spectroscopy
@en
P2093
E B Waygood
J M Scholtz
J W Anderson
P K Hammen
R E Klevit
P2860
P304
P356
10.1002/PRO.5560040513
P577
1995-05-01T00:00:00Z