$\require{mediawiki-texvc}$
  • 검색어에 아래의 연산자를 사용하시면 더 정확한 검색결과를 얻을 수 있습니다.
  • 검색연산자
검색연산자 기능 검색시 예
() 우선순위가 가장 높은 연산자 예1) (나노 (기계 | machine))
공백 두 개의 검색어(식)을 모두 포함하고 있는 문서 검색 예1) (나노 기계)
예2) 나노 장영실
| 두 개의 검색어(식) 중 하나 이상 포함하고 있는 문서 검색 예1) (줄기세포 | 면역)
예2) 줄기세포 | 장영실
! NOT 이후에 있는 검색어가 포함된 문서는 제외 예1) (황금 !백금)
예2) !image
* 검색어의 *란에 0개 이상의 임의의 문자가 포함된 문서 검색 예) semi*
"" 따옴표 내의 구문과 완전히 일치하는 문서만 검색 예) "Transform and Quantization"

과학기술 지식인프라 ScienceON

상세검색 다국어 입력
도움말도움말
쳇봇 이모티콘
안녕하세요!
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

MyON담기
내보내기

Minimally Complex Problem Set for an Ab initio Protein Structure Prediction Study

Biotechnology and bioprocess engineering v.9 no.5 , 2004년, pp.414 - 418  
Kim RyangGug (Interdisciplinary Program for Biochemical Engineering and Biotechnology, College of Engineering, Seoul National University ) ;  Choi Cha-Yong ( Interdisciplinary Program for Biochemical Engineering and Biotechnology, College of Engineering, Seoul National University, School of Chemical Engineering, College of Engineering, Seoul National University)
Abstract

A 'minimally complex problem set' for ab initio protein Structure prediction has been proposed. As well as consisting of non-redundant and crystallographically determined high-resolution protein structures, without disulphide bonds, modified residues, unusual connectivities and heteromolecules, it is more importantly a collection of protein structures. with a high probability of being the same in the crystal form as in solution. To our knowledge, this is the first attempt at this kind of dataset. Considering the lattice constraint in crystals, and the possible flexibility in solution of crystallographically determined protein structures, our dataset is thought to be the safest starting points for an ab initio protein structure prediction study.

주제어

#ab initio protein Structure prediction   #crystal-packing effect   #protein data bank   #data-set  

참고문헌 (18)

  1. Anfinsen, C. B., R. R. Redfield, W. L. Choate, J. Page, and W. R. Carroll (1954) Studies on the gross structure, crosslinkages, and terminal sequences in ribonuclease. J. Biol. Chem. 207: 201-210 
  2. Moult, J. (1999) Predicting protein three-dimensional structure. Curr. Opin. Biotechnol. 10: 583-588 
  3. Sanchez, R. and A. Sali (1998) Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc. Natl. Acad. Sci. USA 95: 13597-13602 
  4. Urbanova, M., R. K. Dukor, P. Pancoska, V. P. Gupta, and T. A. Keiderling (1991) Comparison of alpha-lactalbumin and lysozyme using vibrational circular dichroism. Evidence for a difference in crystal and solution structures. Biochemistry 30: 10479-10485 
  5. Schubert, W. D., G. Gobel, M. Diepholz, A. Darji, D. Kloer, T. Hain, T. Chakraborty, J. Wehland, E. Domann, and D. W. Heinz (2001) Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. J. Mol. BioI. 312: 783-794 
  6. Deuerling, E., H. Patzelt, S. Vorderwulbecke, T. Rauch, G. Kramer, E. Schaffitzel, A. Mogk, A. Schulze-Specking, H. Langen, and B. Bukau (2003) Trigger factor and DnaK possess overlapping substrate pools and binding specificities. Mol. Microbial. 47: 1317-1328 
  7. Shimada, A., O. Nureki, M. Goto, S. Takahashi, and S. Yokoyama (2001) Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase. Proc. Nat. Acad Sci. USA 98: 13537-13542 
  8. Richards, F. M. (1977) Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6: 151-176 
  9. Rodriguez, R., G. Chinea, N. Lopez, T. Pons, and G. Vriend (1998) Homology modeling, model and software evaluation: three related resources. CABIOS 14: 523-528 
  10. Jacobson, M. P., R. A. Friesner, Z. Xiang, and B. Honig (2002) On the role of the crystal environment in determining protein side-chain conformations. J. Mol. Biol. 320: 597-608 
  11. Tsodikov, O. V., M. T. Jr. Record, and Y. V. Sergeev (2002) A novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J. Comput. Chem. 23: 600-609 
  12. Yu, E. W. and D. E. Koshland Jr. (2001) Propagating conformational changes over long (and short) distances in proteins. Proc. Natl. Acad. Sci. USA 98: 9517 -9520 
  13. Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science 181: 223-238 
  14. Gummadi, S. N. (2003) What is the role ofthermodynamics on protein stability. Biotechnol. Bioprocess Eng. 8: 9-18 
  15. Berman, H. M., J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat, H. Weissig, I. N. Shindyalov, and P. E. Bourne (2000) The protein data bank. Nucleic Acids Res. 28: 235-242 
  16. Pearson, W. R. and D. J Lipman. (1988) Improved tools for biological sequence comparison. Proc. Nat! Acad. Sci. USA 85: 2444-2448 
  17. Murzin, A. G., S. E. Brenner, T. Hubbard, and C. Chothia (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247: 536-540 
  18. Ghetu, A. E, M. J. Gubbins, L. S. Frost, and J. N. Glover (2000) Crystal structure of the bacterial conjugation represso finO. Nat. Struct. BioI. 7: 565-569 

이 논문을 인용한 문헌 (0)

  1. 이 논문을 인용한 문헌 없음

원문보기

원문 PDF 다운로드

  • ScienceON :

원문 URL 링크

원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다. (원문복사서비스 안내 바로 가기)

상세조회 0건 원문조회 0건

DOI 인용 스타일