2P029 An Exhaustive Search of Known and Unknown Protein-Ligand Binding Sites with A Fast Alignment-Free Method(The 48th Annual Meeting of the Biophysical Society of Japan)

Artigo Acesso aberto Revisado por pares

2P029 An Exhaustive Search of Known and Unknown Protein-Ligand Binding Sites with A Fast Alignment-Free Method(The 48th Annual Meeting of the Biophysical Society of Japan)

2010; Physical Society of Japan; Volume: 50; Issue: supplement2 Linguagem: Inglês

10.2142/biophys.50.s87_1

ISSN

1347-4219

Autores

Jun‐ichi Ito, Yasuo Tabei, Kana Shimizu, Kentaro Tomii, Koji Tsuda,

Tópico(s)

Chemical Synthesis and Analysis

Resumo

JapanGeneral IncorporatedAssociation the protein is coordmated by two hisudmes (His40 andHis81) one cysteme (Cys78) and one methtontne {Met86) with distorted tetrahedral geometry Recently spectresLopic dnd electreLhemical properties et a site directed mu tdgLnLsis mutant Met16Hls haie been studied In order to furthel exp!ore ot the newly mtroduced His residue of Met16Hb, Mct16HisfHig6Vhl double mutantwasconstructed Perturbation of the ratio of the LMCT bands (A-4Ge!A-.aM]) by the substl tution at Metl6 rLfiects the structural changes around the active site The Tatio A..46o/Any6on of Metl6His and

Ver no editor

Altmetric

PlumX

Entrar

Lembrar minha senha

Receber meu e-mail de confirmação

2P029 An Exhaustive Search of Known and Unknown Protein-Ligand Binding Sites with A Fast Alignment-Free Method(The 48th Annual Meeting of the Biophysical Society of Japan)