Role of cofactors in folding of the blue-copper protein azurin.
about
The Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase †Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding PocketIn vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloproteinIn vitro thermodynamic dissection of human copper transfer from chaperone to target protein.Flexibility of the metal-binding region in apo-cupredoxinsExperimental evidence for a link among cupredoxins: red, blue, and purple copper transformations in nitrous oxide reductase.SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease.Electrochemistry of redox-active self-assembled monolayers.Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Stability and folding behavior analysis of zinc-finger using simple models.Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal: Solvation of azurin's folding nucleus.The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin.The mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli apo-serine hydroxymethyltransferaseModulation of copper site properties by remote residues determines the stability of plastocyanins.Folding and unfolding in the blue copper protein rusticyanin: role of the oxidation state.The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.Comparison of chemical and thermal protein denaturation by combination of computational and experimental approaches. II.Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.Using directed evolution to improve the solubility of the C-terminal domain of Escherichia coli aminopeptidase P. Implications for metal binding and protein stability.Rapid binding of copper(I) to folded aporusticyaninA Copper Story: From Protein Folding and Metal Transport to Cancer
P2860
Q27664258-301E9115-7E97-44D5-9FAC-8205BFBF3D8EQ27675182-4F71ED0B-D31C-4B11-8998-51ABB78FEBDDQ30157456-F2BC6E01-CB05-4203-ACCF-CCFA07CAD7DDQ30160192-2F0C9735-3691-4C5B-B483-D6DF867173DFQ34264580-806D9A44-4440-4794-8570-247D8F90B16BQ36066282-4B04D301-99E3-4520-BA4E-C7ECFE030A84Q36725613-40FE48D7-6C1E-4418-94D2-55B2D55049A4Q37479003-762B7B1B-DCBC-41DC-BC82-82B149D44EA0Q37766457-0701C943-FF95-4E99-B1D1-B36190CE1C9BQ38699291-EBFA1D99-F7DD-4FF3-8239-CA7DB306F51FQ41239653-B15AA0B2-E149-4D64-9EC7-4E70FA0B0AA1Q41788879-A8A0993F-8C5A-4BA1-80C7-56E58C336C6BQ41851138-D17705E7-E2CE-40C0-A272-7313D2420B91Q42025844-D7672071-1A66-49E7-882C-1408CD4AD712Q43028640-A69EDACE-640D-4224-9B99-D05C8E0849FBQ43076740-4A8DCD0A-9B1A-44C0-BE52-4DE813522DFDQ44232333-AD289EEC-8896-43AC-B996-7D249ED6787BQ46631102-2B4CD301-F5E2-4DA1-801E-815A59BCD9A1Q47943726-5758F673-9F95-4FB3-93A2-0C281F9AC2CCQ48235676-7963A2B0-A17B-488C-B33C-2BC1307FB302Q54435819-34DAB995-3A53-4823-8642-DFE2C58A0397Q57673667-BAFD89D6-A6BF-4100-902F-4A45A5F2285BQ57821695-1D23A9DE-6E3A-46F2-BF20-463D11E9C166
P2860
Role of cofactors in folding of the blue-copper protein azurin.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Role of cofactors in folding of the blue-copper protein azurin.
@ast
Role of cofactors in folding of the blue-copper protein azurin.
@en
type
label
Role of cofactors in folding of the blue-copper protein azurin.
@ast
Role of cofactors in folding of the blue-copper protein azurin.
@en
prefLabel
Role of cofactors in folding of the blue-copper protein azurin.
@ast
Role of cofactors in folding of the blue-copper protein azurin.
@en
P356
P1433
P1476
Role of cofactors in folding of the blue-copper protein azurin.
@en
P304
P356
10.1021/IC049398G
P407
P577
2004-12-01T00:00:00Z