Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Biotechnology Letters

• Publication date

  2006-07-06

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1007/s10529-006-9100-0PMID 16823601
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1994influential reference
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  1992influential reference
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  1989cited by this paper
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  1989cited by this paper
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  1987cited by this paper
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  1979influential reference

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