# Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>

**Type:** Papers  
**Canonical URL:** https://scholariq.org/papers/hydrophobic-interaction-at-the-subunit-interface-contributes-to-the/

## Facts

| Field | Value |
| --- | --- |
| Author Names | Hiromi Kirino,Makoto Aoki,Miho Aoshima,Yumiko Hayashi,Masayuki Ohba,Akihiko Yamagishi,Takayoshi Wakagi,Tairo Oshima |
| Citations | 132 |
| DOI | 10.1111/j.1432-1033.1994.tb18623.x |
| Fields | Biochemistry, Genetics and Molecular Biology,Materials Science,Medicine |
| Open Access | false |
| OA Status | closed |
| OpenAlex ID | https://openalex.org/W2053473804 |
| PMID | 8119295 |
| Type | article |
| Year | 1994 |

## Paper authors

- [Makoto Aoki](https://scholariq.org/researchers/makoto-aoki/)

## Paper primary topic

- [Enzyme Structure and Function](https://scholariq.org/topics/enzyme-structure-and-function/)

## Paper topics

- [Enzyme Structure and Function](https://scholariq.org/topics/enzyme-structure-and-function/)
- [Folate and B Vitamins Research](https://scholariq.org/topics/folate-and-b-vitamins-research/)
- [Biochemical and Molecular Research](https://scholariq.org/topics/biochemical-and-molecular-research/)

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Source: ScholarIQ — public research metadata, principally OpenAlex. See https://scholariq.org/sources/ for provenance and https://scholariq.org/methodology/ for what these figures mean.