Investigating structural changes induced by nucleotide binding to RecA using difference FTIR.

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Phosphate binding in the active site of alkaline phosphatase and the interactions of 2-nitrosoacetophenone with alkaline phosphatase-induced small structural changes.

P2860

Q40285478-210AEEF6-B4C2-410E-9EC6-77307B9CABF1

P2860

Investigating structural changes induced by nucleotide binding to RecA using difference FTIR.

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Investigating structural chang ...... to RecA using difference FTIR.

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Investigating structural chang ...... to RecA using difference FTIR.

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Investigating structural chang ...... to RecA using difference FTIR.

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P1476

Investigating structural chang ...... to RecA using difference FTIR.

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P2093

Blaine C Butler

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Gina MacDonald

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Helena Rafailov

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Ross H Hanchett

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P2860

The structure of the E. coli recA protein monomer and polymer

Structure of the recA protein-ADP complex

The use and misuse of FTIR spectroscopy in the determination of protein structure.

The RecA protein: structure and function.

RecA protein: structure, function, and role in recombinational DNA repair.

The mechanism of GTP hydrolysis by Ras probed by Fourier transform infrared spectroscopy.

Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible.

Structural changes of the sarcoplasmic reticulum Ca(2+)-ATPase upon nucleotide binding studied by fourier transform infrared spectroscopy.

DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions.

Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II.

P304

2198-2210

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scholarly article

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10.1016/S0006-3495(02)75566-5

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English

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http://www.w3.org/2001/XMLSchema#string

P478

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2002-04-01T00:00:00Z

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P698

11916875

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P932

1302013

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Investigating structural changes induced by nucleotide binding to RecA using difference FTIR.

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P2860

P2860

Investigating structural changes induced by nucleotide binding to RecA using difference FTIR.

description

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type

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prefLabel

P1433

P1476

P2093

P2860

P304

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P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932