Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2010 Apr 8;6(4):e1000738. doi: 10.1371/journal.pcbi.1000738

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Marcos et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

PMC Copyright notice

(A) Mean hitting time profile for the open and closed (with and without ligands) forms of NAGK. Vertical lines indicate the positions of catalytic (solid line) and ligand-binding residues (dotted line). Note that catalytic residue tend to occupy minima positions, indicative of their efficient communication properties. (B) Difference map between the contribution to hitting times from cross-correlations () (equation (8) in Methods ) of the open and ligand-bound closed forms. Dashed lines set the boundaries of N- and C- domains and also enclose those pairs of domains that undergo the largest changes in the contribution from cross-correlations upon ligand binding. (C) Mean path lengths for linking different parts of the protein: N- and C-domains (blue), N-domain and catalytic site (red), and C-domain and catalytic site (green). (D) Standard deviation in the mean paths displayed in panel (C).

Inline graphic — (A) Mean hitting time profile for the open and closed (with and without ligands) forms of NAGK. Vertical lines indicate the positions of catalytic (solid line) and ligand-binding residues (dotted line). Note that catalytic residue tend to occupy minima positions, indicative of their efficient communication properties. (B) Difference map between the contribution to hitting times from cross-correlations () (equation (8) in Methods ) of the open and ligand-bound closed forms. Dashed lines set the boundaries of N- and C- domains and also enclose those pairs of domains that undergo the largest changes in the contribution from cross-correlations upon ligand binding. (C) Mean path lengths for linking different parts of the protein: N- and C-domains (blue), N-domain and catalytic site (red), and C-domain and catalytic site (green). (D) Standard deviation in the mean paths displayed in panel (C).