Cis proline mutants of ribonuclease A. I. Thermal stability.
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The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroniStatistical Coupling Analysis of Aspartic Proteinases Based on Crystal Structures of the Trichoderma reesei Enzyme and Its Complex with Pepstatin AA cis-Proline in -Hemoglobin Stabilizing Protein Directs the Structural Reorganization of -HemoglobinThe 1.5-A resolution crystal structure of bacterial luciferase in low salt conditionsEngineered β-Lactoglobulin Produced in E. coli: Purification, Biophysical and Structural CharacterisationPressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease AThermodynamic Origin of Prolyl Peptide Bond Isomers.N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin.Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli.Structure and stability of the P93G variant of ribonuclease A.On the non-respect of the thermodynamic cycle by DsbA variants.NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: cis/trans peptide isomerizationThermodynamic characterization of the unfolding of the prion protein.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Protein prosthesis: β-peptides as reverse-turn surrogates.Replacing a single atom accelerates the folding of a protein and increases its thermostability.The crystal structure of the cis-proline to glycine variant (P114G) of ribonuclease A.Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactionsCis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation.Destabilizing mutations alter the hydrogen exchange mechanism in ribonuclease A.Consequences of proline-to-alanine substitutions for the stability and refolding of onconase.Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7.PON-tstab: Protein Variant Stability Predictor. Importance of Training Data Quality.A Study of the Intracellular Routing of Cytotoxic Ribonucleases
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P2860
Cis proline mutants of ribonuclease A. I. Thermal stability.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Cis proline mutants of ribonuclease A. I. Thermal stability.
@en
type
label
Cis proline mutants of ribonuclease A. I. Thermal stability.
@en
prefLabel
Cis proline mutants of ribonuclease A. I. Thermal stability.
@en
P2860
P356
P1433
P1476
Cis proline mutants of ribonuclease A. I. Thermal stability.
@en
P2093
D A Schultz
R L Baldwin
P2860
P304
P356
10.1002/PRO.5560010709
P577
1992-07-01T00:00:00Z