about
Green-lighting green fluorescent protein: Faster and more efficient folding by eliminating acis-transpeptide isomerization eventRandom Single Amino Acid Deletion Sampling Unveils Structural Tolerance and the Benefits of Helical Registry Shift on GFP Folding and StructureStructural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent proteinPeculiarities of the Super-Folder GFP Folding in a Crowded MilieuToward Computationally Designed Self-Reporting Biosensors Using Leave-One-Out Green Fluorescent ProteinExploring the folding pathway of green fluorescent protein through disulfide engineering.Sensitivity of superfolder GFP to ionic agents.Structural Consequences of Chromophore Formation and Exploration of Conserved Lid Residues amongst Naturally Occurring Fluorescent ProteinsBeta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.Distinct effects of guanidine thiocyanate on the structure of superfolder GFP.Structural basis of fluorescence quenching in caspase activatable-GFP.Water Diffusion In And Out Of The β-Barrel Of GFP and The Fast Maturing Fluorescent Protein, TurboGFP.Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome.Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shiftsHeterogeneous side chain conformation highlights a network of interactions implicated in hysteresis of the knotted protein, minimal tied trefoil.Untangling the Influence of a Protein Knot on Folding.Hysteresis as a Marker for Complex, Overlapping Landscapes in Proteins.A rewired green fluorescent protein: folding and function in a nonsequential, noncircular GFP permutantMispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu.Characterization of Split Fluorescent Protein Variants and Quantitative Analyses of Their Self-Assembly Process.Structural Perturbation of Superfolder GFP in the Presence of Guanidine Thiocyanate
P2860
Q27681263-049C58EE-4227-4B29-A65E-9FF7DFC6CB0BQ27683933-D387057D-9CA9-43F4-BFE2-E2B1CEB63EFAQ27684902-97E78F03-E24E-4E19-86AA-1F40CCB77A37Q28818120-7E18431D-2166-42B8-8DEA-E1B9895A297BQ28830732-70CA77B9-5F2D-473D-BDDE-175B134C4030Q30153267-DAC3FEF2-4971-465E-9505-CB32CD2EE581Q30153311-CF416F0A-C34A-43CF-9619-52B464E5F757Q30153444-394D7A5F-F02F-42DD-B5D1-8880B7F4F4D0Q30155144-1618D8A1-F25E-42A0-B3E1-CEF3CED134C4Q30155182-9E41716A-8ED8-4E43-865D-E68E09EF6739Q30155186-3623378B-AE27-4743-B1EF-18D18015CFE9Q30155316-2FD949DB-7298-4D6A-B25F-DEF4A961385CQ30155421-B20E38A0-47D8-4634-9EE9-7419E2B60703Q30360192-C35D3320-3E1F-438D-9175-AD9A0492ACA1Q33762885-F25B01FB-BEB3-4040-9343-14E1C99E868BQ36377435-F7B94387-176D-4EB3-8CF1-3F5806B43302Q36678712-4D779ACC-0561-425B-87AD-1847676AC3C4Q41931577-02E8EC46-AC65-452B-AD18-A932A37A4C15Q42717756-E9EA7BBC-64F5-4B2F-BC61-675BAC80EFBEQ47828633-BD3B2F6F-0415-4E86-BAE0-82D2576FD53CQ55197845-9E9B1A98-B3B6-4FAD-96BC-F90E9832E568Q57908388-6E14ACDE-55BF-4FA1-A2FB-23782048D2F7
P2860
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Chromophore packing leads to hysteresis in GFP.
@en
Chromophore packing leads to hysteresis in GFP.
@nl
type
label
Chromophore packing leads to hysteresis in GFP.
@en
Chromophore packing leads to hysteresis in GFP.
@nl
prefLabel
Chromophore packing leads to hysteresis in GFP.
@en
Chromophore packing leads to hysteresis in GFP.
@nl
P2093
P2860
P1476
Chromophore packing leads to hysteresis in GFP.
@en
P2093
Benjamin T Andrews
Melinda Roy
Patricia A Jennings
P2860
P304
P356
10.1016/J.JMB.2009.06.072
P407
P577
2009-07-03T00:00:00Z