Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
Y Oguchi, H Maeda, K Abe, T Nakajima… - Biotechnology …, 2006 - pubmed.ncbi.nlm.nih.gov
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease.
Y Oguchi, H Maeda, K Abe, T Nakajima… - Biotechnology …, 2006 - search.ebscohost.com
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
Y Oguchi, H Maeda, K Abe, T Nakajima… - Biotechnology …, 2006 - search.proquest.com
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
Y Oguchi, H Maeda, K Abe, T Nakajima, T Uchida… - Biotechnology …, 2006 - infona.pl
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
[引用][C] Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
Y OGUCHI - Biotechnol. Lett., 2006 - cir.nii.ac.jp
Hydrophobic interactions between the secondary structures on the molecular surface
reinforce the alkaline stability of serine protease | CiNii Research CiNii 国立情報学研究所 学術 …
reinforce the alkaline stability of serine protease | CiNii Research CiNii 国立情報学研究所 学術 …
Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease.
Y Oguchi, H Maeda, K Abe, T Nakajima… - Biotechnology …, 2006 - europepmc.org
We employed random mutagenesis to determine the region of the initial unfolding of hyper-
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under …
[引用][C] Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease
Y OGUCHI, H MAEDA, K ABE… - Biotechnology …, 2006 - pascal-francis.inist.fr
Hydrophobic interactions between the secondary structures on the molecular surface
reinforce the alkaline stability of serine protease CNRS Inist Pascal-Francis CNRS Pascal …
reinforce the alkaline stability of serine protease CNRS Inist Pascal-Francis CNRS Pascal …