Structural studies of imidazole-cytochrome c: Resonance assignments and structural comparison with cytochrome c

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Structural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c

Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...

متن کامل

Structural transformation of cytochrome c and apo cytochrome c induced by sulfonated polystyrene.

The structural transformation of cytochrome c (cyt c) and its heme-free precursor, apo cyt c, induced by negatively charged sulfonated polystyrene (SPS) with different charge density (degree of sulfonation) and chain length was studied to understand the factors that influence the folding and unfolding of the protein. SPS forms stable transparent nanoparticles in aqueous solution. The hydrophobi...

متن کامل

1H NMR studies of eukaryotic cytochrome c. Resonance assignments and iron-hexacyanide-mediated electron exchange.

1H NMR resonance assignments in the spectra of horse, tuna, Neurospora crassa and Candida krusei cytochromes c are described. Assignments have been made using NMR double-resonance techniques in conjunction with electron-exchange experiments, spectral comparison of related proteins, and consideration of the X-ray structure of tuna cytochrome c. Resonances arising from 11 residues of horse cytoch...

متن کامل

Ligand Binding and Structural Perturbations in Cytochrome c Peroxidase

Crystal structures of the complexes formed between cytochrome c peroxidase and cyanide, nitric oxide, carbon monoxide, apd fluoride have been determined and refined to 1.85 A. In all four complexes significant changes occur in the distal heme pocket due to movement of Arg-48, His-52, and a rearrangement of active site water molecules. In the cyanide, nitric oxide, and carbon monoxide complexes,...

متن کامل

Fast structural dynamics in reduced and oxidized cytochrome c.

The sub-nanosecond structural dynamics of reduced and oxidized cytochrome c were characterized. Dynamic properties of the protein backbone measured by amide (15)N relaxation and side chains measured by the deuterium relaxation of methyl groups change little upon change in the redox state. These results imply that the solvent reorganization energy associated with electron transfer is small, cons...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics

سال: 1996

ISSN: 0005-2728

DOI: 10.1016/s0005-2728(96)00038-2