From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1cq2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1cq2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1cq2| PDB=1cq2 | SCENE= }} | | {{STRUCTURE_1cq2| PDB=1cq2 | SCENE= }} |
| | | | |
| - | '''NEUTRON STRUTURE OF FULLY DEUTERATED SPERM WHALE MYOGLOBIN AT 2.0 ANGSTROM'''
| + | ===NEUTRON STRUTURE OF FULLY DEUTERATED SPERM WHALE MYOGLOBIN AT 2.0 ANGSTROM=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Although hydrogens comprise half of the atoms in a protein molecule and are of great importance chemically and structurally, direct visualization of them by using crystallography is difficult. Neutron crystallography is capable of directly revealing the position of hydrogens, but its use on unlabeled samples faces certain technical difficulties: the large incoherent scattering of hydrogen results in background scattering that greatly reduces the signal to noise of the experiment. Moreover, whereas the scattering lengths of C, N, and O are positive, that of hydrogen is negative and about half the magnitude. This results in density for hydrogens being half as strong and close to the threshold of detection at 2.0-A resolution. Also, because of its opposite sign, there is a partial cancellation of the hydrogen density with that from neighboring atoms, which can lead to ambiguities in interpretation at medium resolution. These difficulties can be overcome by the use of deuterated protein, and we present here a neutron structure of fully deuterated myoglobin. The structure reveals a wealth of chemical information about the molecule, including the geometry of hydrogen bonding, states of protonation of histidines, and the location and geometry of water molecules at the surface of the protein. The structure also should be of broader interest because it will serve as a benchmark for molecular dynamics and energy minimization calculations and for comparison with NMR studies.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10725379}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10725379 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10725379}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Globular]] | | [[Category: Globular]] |
| | [[Category: Helical]] | | [[Category: Helical]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:59:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:05:33 2008'' |
Revision as of 18:05, 30 June 2008
Template:STRUCTURE 1cq2
NEUTRON STRUTURE OF FULLY DEUTERATED SPERM WHALE MYOGLOBIN AT 2.0 ANGSTROM
Template:ABSTRACT PUBMED 10725379
About this Structure
1CQ2 is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin., Shu F, Ramakrishnan V, Schoenborn BP, Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3872-7. PMID:10725379
Page seeded by OCA on Mon Jun 30 21:05:33 2008
