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Barnase
Backbone Dynamics of Free Barnase and Its Complex with Barstar Determined by 15N NMR Relaxation Study
Characterization of in Vitro Oxidized Barstar
The Folding of Groel-Bound Barnase As a Model for Chaperonin-Mediated Protein Folding (Chaperone/Protein Engineering)
Investigating the Structural Determinants of Electrostatic Binding Among Protein-Protein Complexes: a Systematic, Large-Scale Computational Study
FOR Environmental Release of Genetically Engineered Mustard
A General Approach for the Generation of Orthogonal Trnas
Part II – Summary
Identification and Characterization of Protein Folding Intermediates Stefano Gianni, Ylva Ivarsson, Per Jemth, Maurizio Brunori, Carlo Travaglini-Allocatelli
Spectrin SH3 Domain Xavier Periole,1* Michele Vendruscolo,2 and Alan E
Recombinant Expression of Barnase in Escherichia Coli and Its
Molecular Constructor on the Basis of Barnase–Barstar Module
Adaptation of E. Coli Towards Tryptophan Analog Usage
Using Stochastic Roadmap Simulation to Predict Experimental Quantities in Protein Folding Kinetics: Folding Rates and Phi-Values
Phylogenetic Distribution of Extracellular Guanyl-Preferring Ribonucleases Renews Taxonomic Status of Two Bacillus Strains†
Barnase and Binase: Twins with Distinct Fates Vera Ulyanova, Valentina Vershinina and Olga Ilinskaya
Trimeric Domain-Swapped Barnase (Protein Folding͞trimerization)
At Approval) – Application A1140
Unified Rational Protein Engineering with Sequence-Only Deep Representation Learning
Top View
An L-RNA Aptamer That Binds and Inhibits Rnase
Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles
Understanding the Frustration Arising from the Competition Between Function, Misfolding, and Aggregation in a Globular Protein
Barnase As a New Therapeutic Agent Triggering Apoptosis in Human Cancer Cells
16 23501P A1.Pdf
A New System for Cloning and Expressing Protein-Coding Regions
Structural Characterization of a Misfolded Intermediate Populated During the Folding Process of a PDZ Domain
A Genetic Selection for Compensating Mutations at the Barnase-Barstar Interface
Final Assessment Report Application A372
How Optimal Are the Binding Energetics of Barnase and Barstar?