Microbe

Biochemistry

Berg, Jeremy M.; Tymoczko, John L.; Gatto, Jr., Gregory J.; Stryer, Lubert

8 ed.

New York: W.H. Freeman and Company, 2015

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z  

 34 termes

F0 subunit  n.

p. 543

The F0 subunit is a hydrophobic segment that spans the inner mitochondrial membrane.


F1 subunit  n.

p. 544

The F0 and F subunits are connected in two ways: by the central xgammaxxepsilonx stalk and by an exterior column.


F-2,6-BP  n. (fructose 2,6-biphosphate )

p. 472

The key means by which glycolysis in the liver responds to changes in blood glucose is through the signal molecule fructose 2,6-biphosphate (F-2,6-BP), a potent activator of phosphofructokinase (Figure 16.19).

El sinònim no és neològic.


FADH2  n. (flavin adenine dinucleotide reduced)

p. 526

In oxidative phosphorylation, electrons from NADH and FADH2 are used to reduce molecular oxygen to water.

El sinònim no és neològic.


fast twitch  n.

p. 464

For example, a specific type of muscle fiber, called fast twitch or type IIb fibers, performs short bursts of intense exercise.


fatty acid chain  n.

p. 358

The lenght of the fatty acid chain also affects the transition temperature.


fatty acid metabolism  n.

p. 662

Acetyl CoA carboxylase 2, an isozyme of carboxylase 1 located in the mitochondria, is the essential regulatory enzyme for fatty acid metabolism (Section 22.5).


fatty acid synthesis  n.

p. 664

In the second round of fatty acid synthesis, butyryl ACP condenses with malonyl ACP to form a C6-xbetax-ketoacyl ACP.


FBPase2  n. (fructose biphosphatase 2 )

p. 484

Fructose 6-phosphate is formed through the hydrolysis of fructose 2,6-biphosphate by a specific phosphatase, fructose biphosphatase 2 (FBPase 2).


FDG  n. (2-18F-2-D-deoxyglucose)

p. 475

Figure 16,22 Tumors can be visualized with 2-18F-2-D-deoxyglucose (FDG) and positron emission tomography.


F-dUMP  n. (fluorodeoxyuridylate )

p. 757

Fluorouracil, an anticancer drug, is converted in vivo into fluorodeoxyuridylate (F-dUMP).


feedforward stimulation  n.

p. 472

Glycolysis is thus accelerated when glucose is abundant. Such a process is called feedforward stimulation.


ferredoxin-NADP+  n.

p. 576

Ferredoxin-NADP+ reductase converts NADP+ into NADPH


fibrin monomer  n.

p. 305

Higher-resolution images reveal how the removal of the fibrinopeptides permits the fibrin monomers to come together to form fibrin.


fibrous protein  n.

p. 44

Fibrous proteins provide structural support for cells and tissues


fight-or-flight response  n.

p. 399

In exerts a wide range of effectsxguiollargxreferred to as the fight-or-flight responsexguiollargxto help organisms anticipate the need for rapid muscular activity, including acceleration of heart rate, dilation of the smooth muscle of the airways, and initiation of the breakdown of glycogen (Section 21.3) and fatty acids (Sections 22.2).


filamentous temperature-sensitive mutant Z  n. (FtsZ)

p. 1023

Sequence analysis identified a prokaryotic protein called FtsZ (for filamentous temperature-sensitive mutant Z) that is quite similar to the tubulins.


first cycle  n.

p. 141

FIGURE 5.6 The first cycle in the polymerase chain reaction (PCR). A cycle consists of three steps: DNA double strand separation, the hybridization of primers, and the extension of primers by DNA synthesis.


five-carbon sugar  n.

p. 595

The problem is to construct a five-carbon sugar from six-carbon and three-carbon sugars.


FliG  n.

p. 1027

The proteins FliG, FliM, and FliN are part of a disc-like structure called the MS (membrane and supramembrane) ring, with approximately 30 FliG subunits coming together to form the ring.


FliM  n.

p. 1027

The proteins FliG, FliM, and FliN are part of a disc-like structure called the MS (membrane and supramembrane) ring, with approximately 30 FliG subunits coming together to form the ring.


FliN  n.

p. 1027

The proteins FliG, FliM, and FliN are part of a disc-like structure called the MS (membrane and supramembrane) ring, with approximately 30 FliG subunits coming together to form the ring.


fluorescence micrograph  n.

p. 82

FIGURE 3.21. Fluorescence micrograph of a developing Drosophila embryo.


fluorodeoxyuridylate  n. (F-dUMP)

p. 757

Fluorouracil, an anticancer drug, is converted in vivo into fluorodeoxyuridylate (F-dUMP).


folding funnel  n.

p. 54

The folding funnel depicts the thermodynamics of protein folding.


foreign peptide  n.

p. 1000

Helper T cells stimulate cells that display foreign peptides bound to class II MHC proteins


formyltetrahydrofolate  n.

p. 749

N10-formyltetrahydrofolate donates a formyl moiety to this amino group to form formylglycinamide ribonucleotide.


free amino acid  n.

p. 686

FIGURE 23.7 The proteasome and other proteases generate free amino acids.


free-energy difference  n.

p. 218

To understand how enzymes operate, we need to consider only two thermodynamic properties of the reaction: (1) the free-energy difference (xdeltaxG) between the products and reactants and (2) the energy required to initiate the conversion of reactants into products.


free-energy profile  n.

p. 458

A free-energy profile of the glyceraldehyde 3-phosphate dehydrogenase reaction, compared with a hypothetical process in which the reaction proceeds without this intermediate, reveals how this intermediate allows a favorable process to drive an unfavorable one (Figure 16.6).


fructose biphosphatase 2  n. (FBPase2)

p. 484

Fructose 6-phosphate is formed through the hydrolysis of fructose 2,6-biphosphate by a specific phosphatase, fructose biphosphatase 2 (FBPase 2).


FtsZ  n. (filamentous temperature-sensitive mutant Z)

p. 1023

Sequence analysis identified a prokaryotic protein called FtsZ (for filamentous temperature-sensitive mutant Z) that is quite similar to the tubulins.


fuel oxidation  n.

p. 435

1. Activated Carriers of Electrons for Fuel Oxidation. In aerobic organisms, the ultimate electron acceptor in the oxidation of fuel molecules is O2.


functional effect  n.

p. 152

Recombinant methods enable the exploration of the functional effects of disease-causing mutations