• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Structural Change of Ca^<++>-binding sites in Ca^<++>-binding protein by Solurion X-Ray Scattering

Research Project

Project/Area Number 60480488
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field 結晶学
Research InstitutionOSAKA UNIVERSITY

Principal Investigator

UEKI TATZUO  Faculty of Enginerring Science,Osaka University, 基礎工学部, 助教授 (30029954)

Co-Investigator(Kenkyū-buntansha) INOKO YOJI  Faculty of Engineering Science,Osaka University, 基礎工学部, 教務職員 (00160010)
Project Period (FY) 1985 – 1987
Project Status Completed (Fiscal Year 1987)
Budget Amount *help
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1987: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1986: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1985: ¥5,500,000 (Direct Cost: ¥5,500,000)
KeywordsTroponin C / Solution X-Ray Scattering / Small-angle X-Ray Scattering / Calcium binding protein / 亜鈴型構造のX線散乱 / X線溶液散乱法 / ドメイン構造の散乱 / 亜鈴型構造モデル
Research Abstract

The contraction of muscle is controlled by the Ca^<++>ion concentration in the cell.The protein,that plays an important role in the initial stage of muscle contraction,is troponin C (MW-18,000).The present project is concerned with the structural changes induce by the binding of Ca^<++>ions to troponin C in solution,studied by solution X-ray scattering technique. The results are summarized below.
1.The solution X-ray scattering from troponin C gives a distinct scattering profile in the moderate-angle region,in addition to the small-angle scattering.The profile changes as the binding of Ca^<++>ions to troponin C is controlled.
2.The small-angle scattering from troponin C solution consists of two "Guinier regions"(in a plot of ln[I(S)]vs.S^2).This behavior is throughly described by a Dumbbell-shaped molecule model.The analysis of the scattering profile by a dumbbell-shaped model affords three important structural parameters;The radius of gyration of of troponin C molecule, Rg(molecule),radius of gyration of N-and C-terminal domain of molecule,Rg(domain)and the distance between the centers of domains,r_<n-c>.
3.The Ca^<++>-free troponin C is described by the structural parameters,
Rg(molecule)=27.8A,
Rg(domain)=15.5A,
r_<n-c>=46.3A.
When the troponin C molecules bind with two/four Ca^<++>ions,the N-/C-terminal domain becomes more conpact,i.e.,Rg(domain)decrease from 15.5A-14.8A-14.6A. At the same time,the distance between the domains changes as 46.3A-37.3A-34.5A. This change is,in other words,the change of molecule itself,i.e.,the troponin C molecule becomes more compact as a whole.
These results are in accord with the structure of troponin C molecule that carries two Ca^<++>ions in crystal.

Report

(2 results)
  • 1987 Final Research Report Summary
  • 1986 Annual Research Report
  • Research Products

    (5 results)

All Other

All Publications (5 results)

  • [Publications] T. FUJISAWA: J. Appl. Cryst.20. 349-355 (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1987 Final Research Report Summary
  • [Publications] T. FUJISAWA: J. Biochem.

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1987 Final Research Report Summary
  • [Publications] Tetsuro FUJISAWA: "X-Ray Scattering from a Troponin C Solution and its Interpretation with a Dumbbell-Shaped-Molecule Model." J.Appl.Cryst.20. 349-355 (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1987 Final Research Report Summary
  • [Publications] Tetsuro FUJISAWA: "Ca^<++>-induced Shortening between two Centers of Domains and Decrease of Radii of Domains of Troponin C,Measured by Solution X-ray Scattering." J.Biochem.

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1987 Final Research Report Summary
  • [Publications] Tetsuro FUJISAWA: J.Appl.Cryst.(1987)

    • Related Report
      1986 Annual Research Report

URL: 

Published: 1987-03-31   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi