Truncated staphylococcal nuclease is compact but disordered. - Wikidata - awgldk - TriplyDB

Truncated staphylococcal nuclease is compact but disordered.

Truncated staphylococcal nuclease is compact but disordered.

http://www.wikidata.org/entity/Q31101954

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Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods Delta98Delta, a minimalist model of antiparallel beta-sheet proteins based on intestinal fatty acid binding protein Principles of protein folding--a perspective from simple exact models.Probing the conformational state of a truncated staphylococcal nuclease R using time of flight mass spectrometry with limited proteolysis.The methanol-induced transition and the expanded helical conformation in hen lysozyme.The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent.Unusual compactness of a polyproline type II structure.Protein folding at the exit tunnel.Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease folding Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.The burial of solvent-accessible surface area is a predictor of polypeptide folding and misfolding as a function of chain elongation The topomer search model: A simple, quantitative theory of two-state protein folding kinetics.Cooperativity in protein-folding kinetics.Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease.Interactions in nonnative and truncated forms of staphylococcal nuclease as indicated by mutational free energy changes Surface point mutations that significantly alter the structure and stability of a protein's denatured state Cloning, expression, and purification of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase: crystallization of nucleic acid complexes.Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics Solution structures of RseA and its complex with RseB Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins Systematic alanine insertion reveals the essential regions that encode structure formation and activity of dihydrofolate reductase.Random-coil behavior and the dimensions of chemically unfolded proteins.The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase.Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Protein conformational switches: from nature to design.Non-sequence-specific interactions can account for the compaction of proteins unfolded under "native" conditions.Cytochrome unfolding pathways from computational analysis of crystal structures.Protein folding in high-dimensional spaces: hypergutters and the role of nonnative interactions.Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.Nonlocal interactions are responsible for tertiary structure formation in staphylococcal nuclease.Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor.Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding.NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study.Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

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P2860

Truncated staphylococcal nuclease is compact but disordered.

http://www.wikidata.org/entity/Q31101954

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1992 nî lūn-bûn

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1992 թուականի Յունուարին հրատարակուած գիտական յօդուած

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1992 թվականի հունվարին հրատարակված գիտական հոդված

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1992年の論文

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1992年論文

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1992年論文

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1992年論文

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1992年論文

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1992年論文

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1992年论文

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Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

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

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Truncated staphylococcal nuclease is compact but disordered.

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P2093

Engelman DM

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Flanagan JM

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Kataoka M

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Shortle D

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P2860

The formation and stabilization of protein structure

The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A

Theory for the folding and stability of globular proteins

Dominant forces in protein folding

Melittin binding causes a large calcium-dependent conformational change in calmodulin.

Transient folding intermediates characterized by protein engineering.

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

Kinetic and magnetic resonance studies of effects of genetic substitution of a Ca2+-liganding amino acid in staphylococcal nuclease.

Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution.

Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

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2

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