Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures.
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A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroThe design and characterization of two proteins with 88% sequence identity but different structure and functionStructure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein designTryptophan zippers: Stable, monomeric -hairpinsNMR structures of two designed proteins with high sequence identity but different fold and functionDisorder and Structure in the Rab11 Binding Domain of Rab11 Family Interacting Protein 2 † ‡A minimal sequence code for switching protein structure and functionFolding thermodynamics of protein-like oligomers with heterogeneous backbonesCrystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomainUse of a zinc-finger consensus sequence framework and specificity rules to design specific DNA binding proteinsA Dynamic Model of pH-Induced Protein G'e Higher Order Structure Changes derived from Mass Spectrometric AnalysesSequence of events in folding mechanism: beyond the Gō modelThe design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysisCloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima.Thermal unfolding of small proteins with SH3 domain folding pattern.Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches.Reduced native state stability in crowded cellular environment due to protein-protein interactionsCAPITO--a web server-based analysis and plotting tool for circular dichroism data.Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation.Conformational studies of the alpha-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Stabilizing the subtilisin BPN' pro-domain by phage display selection: how restrictive is the amino acid code for maximum protein stability?Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. I. Importance of hydrophobic interactions in stabilization of beta-hairpin structure.How micro-phase separation alters the heating rate effects on globular protein gelation.Residue level quantification of protein stability in living cells.Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation.Are proteins well-packed?Structure of a switchable subtilisin complexed with a substrate and with the activator azideSubdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.Structural and functional characterization of the recombinant death domain from death-associated protein kinase."De-novo" amino acid sequence elucidation of protein G'e by combined "top-down" and "bottom-up" mass spectrometry.Length-encoded multiplex binding site determination: application to zinc finger proteinsThermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation.Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G.Surface point mutations that significantly alter the structure and stability of a protein's denatured stateThe calorimetric criterion for a two-state process revisitedThe role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.Single-molecule fluorescence studies of protein folding and conformational dynamicsComparison of (13)C(alpha)H and (15)NH backbone dynamics in protein GB1.
P2860
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P2860
Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Thermodynamic analysis of the ...... igh denaturation temperatures.
@en
type
label
Thermodynamic analysis of the ...... igh denaturation temperatures.
@en
prefLabel
Thermodynamic analysis of the ...... igh denaturation temperatures.
@en
P2093
P356
P1433
P1476
Thermodynamic analysis of the ...... igh denaturation temperatures.
@en
P2093
P304
P356
10.1021/BI00129A007
P407
P577
1992-04-01T00:00:00Z