Add to ORKGA new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horsehemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states
Mammalian haemoglobins undergo a reversible transition between two alternative structures. One of th...
The geminate recombination kinetics of CO-myoglobin strongly deviates from single exponential behavi...
We have extended the method of modulated excitation, a small perturbation kinetic method, to study l...
The crystal structure of high-salt horse methaemoglobin has been determined at environmental relativ...
There has been considerable interest in the variability of the structure of the liganded haemoglobin...
There has been considerable interest in the variability of the structure of the liganded haemoglobin...
This paper describes E new method of producing a crystalline intermediate between the unligated and ...
In this work the hemoglobin conformational changes induced by changing the iron charge have been stu...
In hemoproteins the relaxation mechanism of iron is Orbach for high spin (HS) and Raman for low spin...
Haemoglobin (Hb) is an iron-containing metalloprotein which plays a major role in the transportation...
High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at different levels of envir...
In X-band electron paramagnetic resonance spectra from single crystals of horse ferric hemoglobin, o...
The in vitro behavior of various states of hemoglobin was examined over a wide range of concentratio...
We report on a study of the early relaxation processes of met-Myoglobin in aqueous solution, using a...
In this work, initial crystallographic studies of human haemoglobin (Hb) crystallized in isoionic an...
Mammalian haemoglobins undergo a reversible transition between two alternative structures. One of th...
The geminate recombination kinetics of CO-myoglobin strongly deviates from single exponential behavi...
We have extended the method of modulated excitation, a small perturbation kinetic method, to study l...
The crystal structure of high-salt horse methaemoglobin has been determined at environmental relativ...
There has been considerable interest in the variability of the structure of the liganded haemoglobin...
There has been considerable interest in the variability of the structure of the liganded haemoglobin...
This paper describes E new method of producing a crystalline intermediate between the unligated and ...
In this work the hemoglobin conformational changes induced by changing the iron charge have been stu...
In hemoproteins the relaxation mechanism of iron is Orbach for high spin (HS) and Raman for low spin...
Haemoglobin (Hb) is an iron-containing metalloprotein which plays a major role in the transportation...
High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at different levels of envir...
In X-band electron paramagnetic resonance spectra from single crystals of horse ferric hemoglobin, o...
The in vitro behavior of various states of hemoglobin was examined over a wide range of concentratio...
We report on a study of the early relaxation processes of met-Myoglobin in aqueous solution, using a...
In this work, initial crystallographic studies of human haemoglobin (Hb) crystallized in isoionic an...
Mammalian haemoglobins undergo a reversible transition between two alternative structures. One of th...
The geminate recombination kinetics of CO-myoglobin strongly deviates from single exponential behavi...
We have extended the method of modulated excitation, a small perturbation kinetic method, to study l...