Stabilization of phage T4 lysozyme by engineered disulfide bonds - Wikidata - awgldk - TriplyDB

Stabilization of phage T4 lysozyme by engineered disulfide bonds

Stabilization of phage T4 lysozyme by engineered disulfide bonds

http://www.wikidata.org/entity/Q34300374

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Lessons from the lysozyme of phage T4 Simple evolutionary pathways to complex proteins Simulating evolution by gene duplication of protein features that require multiple amino acid residues Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating Stereoelectronic and steric effects in side chains preorganize a protein main chain Cysteine-free rop: A four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics Introduction of a disulfide bond leads to stabilization and crystallization of a ricin immunogen Structural and Mechanistic Studies of Pesticin, a Bacterial Homolog of Phage Lysozymes Mechanism of Protein Kinetic Stabilization by Engineered Disulfide Crosslinks Structural mimicry of a native protein by a minimized binding domain Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A Modulating protein folding rates in vivo and in vitro by side-chain interactions between the parallel beta strands of green fluorescent protein.Insertion of foreign T cell epitopes in human tumor necrosis factor alpha with minimal effect on protein structure and biological activity.Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability.Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C.Effects of disulfide bonds on folding behavior and mechanism of the beta-sheet protein tendamistat.Disulfide by Design 2.0: a web-based tool for disulfide engineering in proteins Computationally designed libraries for rapid enzyme stabilization.Stabilization of cyclohexanone monooxygenase by a computationally designed disulfide bond spanning only one residue.Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-Coupled Receptor Crystallogenesis.Additional disulfide bonds in insulin: Prediction, recombinant expression, receptor binding affinity, and stability.Strong DNA binding by covalently linked dimeric Lac headpiece: evidence for the crucial role of the hinge helices.Enhancing protein stability with extended disulfide bonds.Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase-2.alpha-Amylases and approaches leading to their enhanced stability.Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe Crystallization and preliminary X-ray crystallographic analysis of the oxysterol-binding protein Osh3 from Saccharomyces cerevisiae.Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding Experimental determination of the vertical alignment between the second and third transmembrane segments of muscle nicotinic acetylcholine receptors Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation.Knotted and topologically complex proteins as models for studying folding and stability.Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration The role of thiols and disulfides on protein stability.Implication of disulfide bridge induced thermal reversibility, structural and functional stability for luciferase.

P2860

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P2860

Stabilization of phage T4 lysozyme by engineered disulfide bonds

http://www.wikidata.org/entity/Q34300374

description

1989 nî lūn-bûn

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1989 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1989 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1989年の論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年论文

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name

Stabilization of phage T4 lysozyme by engineered disulfide bonds

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Stabilization of phage T4 lysozyme by engineered disulfide bonds

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Stabilization of phage T4 lysozyme by engineered disulfide bonds

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type

label

Stabilization of phage T4 lysozyme by engineered disulfide bonds

@ast

Stabilization of phage T4 lysozyme by engineered disulfide bonds

@en

Stabilization of phage T4 lysozyme by engineered disulfide bonds

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prefLabel

Stabilization of phage T4 lysozyme by engineered disulfide bonds

@ast

Stabilization of phage T4 lysozyme by engineered disulfide bonds

@en

Stabilization of phage T4 lysozyme by engineered disulfide bonds

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PNAS.86.17.6562

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Stabilization of phage T4 lysozyme by engineered disulfide bonds

@en

P2093

B W Matthews

http://www.w3.org/2001/XMLSchema#string

M Levitt

http://www.w3.org/2001/XMLSchema#string

M Matsumura

http://www.w3.org/2001/XMLSchema#string

W J Becktel

http://www.w3.org/2001/XMLSchema#string

P2860

Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid

Rapid and efficient site-specific mutagenesis without phenotypic selection

The Protein Data Bank: a computer-based archival file for macromolecular structures

Integrating the equations of motion

Protein stability curves

Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

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6562-6566

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scholarly article

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10.1073/PNAS.86.17.6562

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17

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1989-09-01T00:00:00Z

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2671995

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