Nitrate reductase

Homodimers, two identical subunits

Each subunit with 100kD

Each subunit contains 3 prosthetic groups:

FAD, heme, and molybdenum complexed to pterin (an organic molecule). 

TLS Online TPP Program

#Id: 9294

#XL - Q Biochemistry

Nitrate reductase

Homodimers, two identical subunits

Each subunit with 100kD

Each subunit contains 3 prosthetic groups:

FAD, heme, and molybdenum complexed to pterin (an organic molecule). 

TLS Online TPP Program

#Id: 9294

#XL - S Microbiology

Nitrate reductase

Homodimers, two identical subunits

Each subunit with 100kD

Each subunit contains 3 prosthetic groups:

FAD, heme, and molybdenum complexed to pterin (an organic molecule). 

TLS Online TPP Program

#Id: 8539

#XL - Q Biochemistry

The short (∼20 amino acid) C-terminal tails of both α- and β-tubulin that protrude from the microtubule are enriched in glutamic and aspartic acids, the surface of the microtubule possesses a net negative charge.

TLS Online TPP Program

#Id: 8538

#XL - Q Biochemistry

Microtubules can be stabilized by side-binding microtubule associated proteins (MAPs).

TLS Online TPP Program

#Id: 8537

#XL - Q Biochemistry

Augmin-induced branches help build the spindle during mitosis.

TLS Online TPP Program

#Id: 8536

#XL - Q Biochemistry

Plant cells rely extensively on augmin-dependent microtubule branching nucleation to organize the microtubule cytoskeleton because they lack centrosomes.

TLS Online TPP Program

#Id: 8535

#XL - Q Biochemistry

Augmin

an 8-subunit protein complex that binds to sites along the microtubule and recruits γ-TuRC, which nucleates a new microtubule to form a microtubule branch.

TLS Online TPP Program

#Id: 8534

#XL - Q Biochemistry

γ-tubulin ring complex (γ-TuRC)

nucleates assembly of a microtubule by forming a template corresponding to the (−) end.