Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.
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NMR solution structure of the activation domain of human procarboxypeptidase A2The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthusNon-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins.Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.Intramolecular cohesion of coils mediated by phenylalanine--glycine motifs in the natively unfolded domain of a nucleoporin.Correlations between internal mobility and stability of globular proteins.Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitorNeutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability.Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor.The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.The effect of low temperatures on enzyme activity.The denaturation and degradation of stable enzymes at high temperatures.Protein stability and molecular adaptation to extreme conditions.Functionality and the evolution of marginal stability in proteins: inferences from lattice simulationsProteins under extreme physical conditions.Rigidity versus flexibility: the dilemma of understanding protein thermal stability.Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase.The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide.Nativelike enzyme properties are important for optimum activity in neat organic solventsNative protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability.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.In silico evaluation of the resistance of the T790M variant of epidermal growth factor receptor kinase to cancer drug Erlotinib.Hydrogen-deuterium exchange in bovine serum albumin protein monitored by Fourier transform infrared spectroscopy, part II: kinetic studies.Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes.Anabaenaapoflavodoxin hydrogen exchange: On the stable exchange core of the α/β(21345) flavodoxin-like family
P2860
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P2860
Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年論文
@yue
1979年論文
@zh-hant
1979年論文
@zh-hk
1979年論文
@zh-mo
1979年論文
@zh-tw
1979年论文
@wuu
1979年论文
@zh
1979年论文
@zh-cn
name
Correlation between the amide ...... pancreatic trypsin inhibitor.
@en
type
label
Correlation between the amide ...... pancreatic trypsin inhibitor.
@en
prefLabel
Correlation between the amide ...... pancreatic trypsin inhibitor.
@en
P1476
Correlation between the amide ...... pancreatic trypsin inhibitor.
@en
P2093
P356
10.1016/0022-2836(79)90550-3
P407
P577
1979-05-01T00:00:00Z