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Comparative Study of Enzyme Thermostability using Torsion Potentials in the Region of β-Turn

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  • 발행기관
    한국생물공학회 바로가기
  • 간행물
    한국생물공학회 학술대회 바로가기
  • 통권
    2009 추계학술대회 및 국제심포지움 (2009.11)바로가기
  • 페이지
    pp.167-167
  • 저자
    Hong Seung YEON, Young Je YOO
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A115050

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원문정보

초록

영어
Comparative Study of Enzyme Thermostability using Torsion Potentials in the Region of β-Turn Hong Seung Yeon and Young Je YooSchool of Chemical and Biological Engineering, Seoul
National University, Seoul 151-744, Korea Thermostable enzyme has been a key research topic
because it industrially gives a number of beneficial advantages. Various strategies to enhance
thermostability of enzymes have been proposed, however, an integrated strategy has not yet
reported. In this study, torsion potentials in the region of β-turn, as one of strategy to explain
enzyme thermostability, were analyzed between thermophilic and mesophilic enzymes. β-turn is
an element of secondary structure which consists of four residues and plays an important role in
protein structure directing folding pathways. The hypothesis of this study is that it might act to
enhance thermostability of enzymes by introducing favorable torsion angle in the region of β-turn
because β-turn is passively formed by other secondary structures. Thus, it may be assumed that
torsion potential of β-turns in mesophilic enzyme is bigger than thermophilic one. To demonstrate
this hypothesis, thirty sets of thermophlic and mesophilic enzyme pair were chosen through
several qualified criteria and intrinsic torsion potential equation was used. The statistical analysis
showed that torsion potential of mesophilic enzymes in the region of β-Turn is bigger than
thermophilic one at less than 5% level of significance. From this statistical result, optimizing
torsion angle in the region of β-turn can be used as a strategy for enhancing thermostability of
enzymes. ReferencesVijaya Parthiban, M. Michael Gromiha, Christian Hoppe, and Dietmar
Schomburg. PROTEINS:Structure, Function, and Bioinformatics 66:41-52(2007)Young Kee Kang, Kyoung Tai No, and Harold A. Scheraga. J. Phys. Chem 1996, 100, 15588-15598Saul R. Trevino, Stephanie Schaefer, J. Martin Scholtz, and C. Nick Pace. J Mol Biol. 2007 October 12; 373(1): 211-218

키워드

thermostability torsion beta turn

저자

  • Hong Seung YEON [ Dept. of Chemical and Biological Engineering, Seoul National University ]
  • Young Je YOO [ Dept. of Chemical and Biological Engineering, Seoul National University, ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
  • 설립연도
    1984
  • 분야
    공학>생물공학
  • 소개
    이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다 1. 생물공학 분야의 발전을 위한 연구 협력 2. 생물공학의 실용화를 촉진시키기 위한 산학 협동 3. 학술연구 발표회, 강연회, 연수회 등 학술활동의 개최 4. 국,영문 학술지,소식지,학술회의 Proceedings 및 학술도서의 발간 5. 생물공학 발전을 위한 정책 건의 6. 기타 국제 교류 등 본 학회의 목적 달성을 위한 제반 활동

간행물

  • 간행물명
    한국생물공학회 학술대회
  • 간기
    반년간
  • 수록기간
    1985~2013
  • 십진분류
    KDC 476 DDC 576

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