1ajh

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{{STRUCTURE_1ajh| PDB=1ajh | SCENE= }}
{{STRUCTURE_1ajh| PDB=1ajh | SCENE= }}
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'''PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K'''
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===PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K===
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==Overview==
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Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.
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(as it appears on PubMed at http://www.pubmed.gov), where 7634074 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7634074}}
==About this Structure==
==About this Structure==
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[[Category: Photoproduct intermediate]]
[[Category: Photoproduct intermediate]]
[[Category: Respiratory protein]]
[[Category: Respiratory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:21:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:58:55 2008''

Revision as of 13:58, 30 June 2008

Template:STRUCTURE 1ajh

PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K

Template:ABSTRACT PUBMED 7634074

About this Structure

1AJH is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K., Teng TY, Srajer V, Moffat K, Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074

Page seeded by OCA on Mon Jun 30 16:58:55 2008

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