Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions. - Wikidata - wikimedia - TriplyDB

Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions.

Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions.

http://www.wikidata.org/entity/Q41837248

about

Cofactor engineering for enhancing the flux of metabolic pathways 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 Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy Escherichia coli Free Radical-Based Killing Mechanism Driven by a Unique Combination of Iron Restriction and Certain Antibiotics.Protein phosphorylation corrects the folding defect of the neuroblastoma (S120G) mutant of human nucleoside diphosphate kinase A/Nm23-H1.Protein folding in the cell envelope of Escherichia coli.Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants.Ion mobility spectrometry focusing on speciation analysis of metals/metalloids bound to carbonic anhydrase.Inhibitor-mediated stabilization of the conformational structure of a histone deacetylase-like amidohydrolase.Effects of zinc binding on the structure and thermal stability of camel alpha-lactalbumin

P2860

Q26825673-F9BB9353-A1DB-4F0A-9973-14CCFF9A0626 Q35180679-232E81A3-0CA4-4E2E-AE2B-7BAA8E479345 Q36090136-3DB1530A-2200-42D6-BF54-BD58EDEA663E Q36227416-7A22AEC4-4160-48BC-9370-2251F03E4F1B Q38306715-E061FBFA-DE1B-4269-8711-4C6A002B9868 Q38940176-179B556F-8026-4017-B176-78E2848A3F94 Q39618799-AFA1DB6A-4BAA-4E12-A4F3-C0D607E46FDB Q44792787-B6156504-DBF7-46B1-8860-9D766F9A41E4 Q50956825-B8A79D1B-9985-43DC-96DD-6501378D76C6 Q57691278-030D3986-3F38-483C-9518-F7092BC9374C

P2860

Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions.

http://www.wikidata.org/entity/Q41837248

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

Cofactor effects on the protei ...... bumin refolding by metal ions.

@en

type

label

Cofactor effects on the protei ...... bumin refolding by metal ions.

@en

prefLabel

Cofactor effects on the protei ...... bumin refolding by metal ions.

@en

P1433

Q41837248-8609C88A-B53F-4D51-9E1D-744732EA8A72

P1476

Q41837248-E77C4E5A-405D-4288-AA34-A0C3751B5043

P2093

Q41837248-39668D2D-2040-4C78-9FE5-BC656DEEBC54

Q41837248-7808E1E5-8997-4B6D-BB13-26E815698FC0

Q41837248-98922048-CAAD-430F-8B3A-5774BF95AC06

Q41837248-BB2AD284-7CD6-4DA0-B730-2426647723CC

P2860

Q41837248-03000E1F-B1C9-4D44-91F5-D89ECEBBAFA2

Q41837248-191864F5-AC08-4A08-B1B3-1FFF6F57E1E0

Q41837248-211E64F2-041E-4753-A15B-10FC677C1B66

Q41837248-23D3552C-4437-45DC-9720-0DAFEB4E8EAE

Q41837248-44758862-9B5E-478F-88D4-E2035C7F231B

Q41837248-54468402-25B9-4402-BB7B-4FB415FB61F3

Q41837248-61C3CBA4-C900-4100-A42D-D2B2082CE67C

Q41837248-641C60CC-DA6A-4960-9141-43A58862E3F9

Q41837248-671D7149-AE9C-4D15-8388-E7313791DDBE

Q41837248-6D4173B7-A713-4EAD-81DB-3A3E823331A4

P304

Q41837248-09338A47-DF67-45FA-8A94-72375B6534DD

P31

Q41837248-958D34F3-2639-4287-9262-69B28A337785

P356

Q41837248-A7DB5555-0469-4203-9AE4-AB095D0F14A6

P433

Q41837248-E49B7D03-DE03-45A7-8844-C859C3B3AE58

P478

Q41837248-00D87C4C-1D23-4591-8983-4E02956B5B4A

P577

Q41837248-B2B65C7E-1CB7-47C8-8985-3834560E01E7

P5875

Q41837248-A4A05EFD-F95D-4D8C-9623-529729E2E971

P698

Q41837248-004820B0-AE82-41E0-9CD1-26600CEDB9FD

P921

Q41837248-20831BAF-9577-4179-990F-0BA406985CED

Q41837248-F1EA51DC-BB13-4610-B77F-E5D524577777

P932

Q41837248-637A7997-DBA7-48D2-8CCE-45263C7AAADA

P356

P1433

Protein Science

P1476

Cofactor effects on the protei ...... bumin refolding by metal ions.

@en

P2093

Clément E Blanchet

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

Grégory Vernier

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

Natalia A Bushmarina

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

Vincent Forge

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

P2860

Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2. 2-A resolution reveal an effect of calcium on inter-lobe interactions

Divalent metal cofactor binding in the kinetic folding trajectory ofEscherichia coliribonuclease HI

Understanding protein folding via free-energy surfaces from theory and experiment

alpha-Lactalbumin: structure and function

From Levinthal to pathways to funnels

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state.

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.

Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.

Thermodynamic data on the binding of six M2(+)-ions to bovine, goat, and human alpha-lactalbumin.

P304

659-671

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

P31

scholarly article

P356

10.1110/PS.051904206

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

P433

4

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

P478

15

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

P577

2006-03-07T00:00:00Z

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

P5875

7255097

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

P698

16522796

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

P921

protein folding

P932

2242491

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