BROWSE

Related Scientist

Researcher

이효철
나노물질 및 화학반응 연구단
more info

Protein energy landscapes determined by five-dimensional crystallography

Cited 18 time in webofscience Cited 0 time in scopus
544 Viewed 20 Downloaded
Title
Protein energy landscapes determined by five-dimensional crystallography
Author(s)
Schmidt, M.; Srajer, V.; Henning, R.; Hyot Cherl Ihee; Purwar, N.; Tenboer, J.; Tripathi, S.
Publication Date
2013-12
Journal
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.69, no.12, pp.2534 - 2542
Publisher
WILEY-BLACKWELL
Abstract
Free energy landscapes decisively determine the progress of enzymatically catalyzed reactions1. Timeresolved macromolecular crystallography unifies transient-state kinetics with structure determination2-4 because both can be determined from the same set of X-ray data. We demonstrate here how barriers of activation can be determined solely from five-dimensional crystallography5. Directly linking molecular structures with barriers of activation between them allows for gaining insight into the structural nature of the barrier. We analyze comprehensive time series of crystallographic data at 14 different temperature settings and determine entropy and enthalpy contributions to the barriers of activation. 100 years after the discovery of X-ray scattering, we advance X-ray structure determination to a new frontier,the determination of energy landscapes.
URI
https://pr.ibs.re.kr/handle/8788114/1203
ISSN
0907-4449
Appears in Collections:
Center for Nanomaterials and Chemical Reactions(나노물질 및 화학반응 연구단) > Journal Papers (저널논문)
Files in This Item:
258. Protein energy landscapes determined.pdfDownload

qrcode

  • facebook

    twitter

  • Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse