Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.
about
Interactions of cardiolipin and lyso-cardiolipins with cytochrome c and tBid: conflict or assistance in apoptosisCytochrome c/cardiolipin relations in mitochondria: a kiss of deathFörster Resonance Energy Transfer and Conformational Stability of Proteins: An Advanced Biophysical Module for Physical Chemistry StudentsProbing stability and dynamics of proteins by protease digestion. I: Comparison of protease susceptibility and thermal stability of cytochromes c.Protein structure evolution in liquid DESI as revealed by selective noncovalent adduct protein probing.A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale.'Molten-globule state': a compact form of globular proteins with mobile side-chains.Kinetics and mechanism of heme-induced refolding of human alpha-globin.Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.Fast folding of cytochrome cRefolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.Cytochrome c folds through a smooth funnelLeast activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism.Rapid perturbation of free-energy landscapes: from in vitro to in vivo.Effect of sodium dodecyl sulfate on folding and thermal stability of acid-denatured cytochrome c: a spectroscopic approach.Porphyrin fluorescence dominates UV photoemission of folded cytochrome c.Selectivity and Reactivity of Zr and Ce Substituted Keggin Type Polyoxometalates Toward Cytochrome c in Surfactant Solutions
P2860
Q23923071-8D3C46E4-B052-4A51-A082-54347AF250A7Q23923181-DB532481-305F-497E-ACF7-57F46A53204DQ30380723-195A21D5-ABFE-4A18-AB21-8F64261F60B5Q30402563-56C2534C-03FB-4614-A570-BADB659285FFQ30428670-2AD116D9-9000-4560-9B33-8955B4C8A31FQ34167994-E4CBEBB9-F447-47F1-A0A9-CDAA989542B2Q34255230-655D9A4F-9DFE-4804-BF8D-6520536BF481Q35415087-A8297A62-763A-426A-A716-87E8D33B50B8Q36199183-9B110C16-81AC-4D59-BEA3-3C086FD62AE1Q36280325-055325E1-9F07-4558-9699-A402CBEBEDEBQ36280975-AA8BBF9D-BC3D-46D0-A866-E8B30E867401Q36281933-88E2B28A-EF51-4A66-B3CD-C83998DAD226Q37697261-EAC4CB90-3396-4A91-A462-5D0F6DE7272DQ39627108-CADDC626-4CB8-4754-93CD-7310955BB68BQ42121807-25C44915-7150-4CC5-A774-8377FB87944FQ46889846-1A3DB1FE-667F-42EB-9156-17E3EE8951C6Q58698234-8257A6F6-9629-44BA-B7C7-E5A062BA7190
P2860
Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.
description
1976 nî lūn-bûn
@nan
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
1976年论文
@zh
1976年论文
@zh-cn
name
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@en
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@nl
type
label
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@en
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@nl
prefLabel
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@en
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@nl
P356
P1433
P1476
Ferricytochrome c chain foldin ...... yptophan 59 to the heme group.
@en
P2093
P304
P356
10.1021/BI00670A007
P407
P577
1976-12-01T00:00:00Z