Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551. - Wikidata - wikimedia - TriplyDB

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

http://www.wikidata.org/entity/Q41949265

about

The chemistry and biochemistry of heme c: functional bases for covalent attachment Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552 Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551: structural insights into domain swapping of cytochrome c family proteins Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination.Cytochrome unfolding pathways from computational analysis of crystal structures.Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.Studies of cytochrome c-551 unfolding using fluorescence correlation spectroscopy and other biophysical techniques.

P2860

Q24658226-368D0C27-6B8D-4453-814E-ABB9E6A085DE Q27666582-A02F0B3C-0C18-4A78-B70C-C860A44D9459 Q28386311-1A4AA555-1552-4F1E-AF6F-F8F5C50FE950 Q30352565-1DFFC4AC-3A6E-4A12-B25B-A1A129A68A9D Q30373495-EB2EEB59-97B6-4D9C-A921-0FEE946B6B75 Q30403510-DF80DB0F-549E-4343-919A-62C4B5942ED5 Q37826803-E04AED6D-5DCB-45CF-854F-E7BE56A25FAC Q40276181-157DCE43-D5F1-4E27-A961-6A1E4A464FEF Q42623250-429C1B22-294F-4E72-B64A-CD3300ED59CF Q51563620-407F2631-9D4B-4ED2-95CB-500403BCF4D2

P2860

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

http://www.wikidata.org/entity/Q41949265

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

@en

type

label

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

@en

prefLabel

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

@en

P1433

Q41949265-3D5F6A54-E74F-4373-8BD5-E17EFA586F3A

P1476

Q41949265-D36D6BD9-5CEC-4319-A0AB-25080DD8D32E

P2093

Q41949265-72BB0303-1652-4237-8745-824113A51FD2

P2860

Q41949265-11E923FA-5E72-4C75-B4B8-FAD741C29EC3

Q41949265-1D4A37D8-A6C3-4646-94F1-50A174D3CA9C

Q41949265-1E3F4527-D716-4E2A-ABD1-01DA30B9BD1C

Q41949265-2217DB3D-9F5B-4CDB-A91B-C58ADBA1C36E

Q41949265-2399F9AE-29EC-4622-AFCC-EF1B12F893F6

Q41949265-25C295FC-95E0-444F-A0BD-C5625F43685C

Q41949265-3007E78D-19F9-4164-9C73-EDE727D3A7DC

Q41949265-39AEFEE9-1688-4CA7-9781-C148A5094690

Q41949265-3E8616FB-9898-4EA7-9CE7-D04FB19A6A3E

Q41949265-40BF4209-4D49-4B0B-B5CE-BC610C872456

P2888

Q41949265-D100E7FE-A7F4-4E12-B203-D1D07625327D

P304

Q41949265-114897A1-E8F1-4E00-91FC-DE2C7BE5EBC1

P31

Q41949265-948B98C2-B940-440E-BBD9-187413C35A03

P356

Q41949265-793C9BCB-7F7E-4ED8-B411-9E5CC5354A4C

P433

Q41949265-6B3FD3DB-EF00-4EAA-9FC6-58842DFDD44B

P478

Q41949265-51103681-EB83-44C5-A6D4-9F9D130E2018

P50

Q41949265-D2FEAE52-9C58-4FBC-B0DC-1D2757A248A8

P577

Q41949265-780F8CCE-D12C-45FD-B0D2-FEA9D9A736C2

P5875

Q41949265-7D12028F-FFAF-4547-9BB0-A495B6685999

P698

Q41949265-9E03411B-4020-441A-8F30-3A9658FA0053

P932

Q41949265-C6269702-75FE-43E9-885A-8E444B88FEEB

P356

S00775-008-0370-Y

P1433

Journal of Biological Inorganic Chemistry

P1476

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.

@en

P2093

Lea V Michel

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

P2860

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c

High-resolution three-dimensional structure of horse heart cytochrome c

Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms

Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site.

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

From Levinthal to pathways to funnels

Refolding kinetics of cytochrome c(551) reveals a mechanistic difference between urea and guanidine

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Primary structure effects on peptide group hydrogen exchange

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

P2888

s00775-008-0370-y

P304

837-845

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

P31

scholarly article

P356

10.1007/S00775-008-0370-Y

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

P433

5

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

P478

13

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

P50

P577

2008-04-08T00:00:00Z

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

P5875

5459513

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

P698

18392863

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

P932

2654780

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