1answer.
Ask question
Login Signup
Ask question
All categories
  • English
  • Mathematics
  • Social Studies
  • Business
  • History
  • Health
  • Geography
  • Biology
  • Physics
  • Chemistry
  • Computers and Technology
  • Arts
  • World Languages
  • Spanish
  • French
  • German
  • Advanced Placement (AP)
  • SAT
  • Medicine
  • Law
  • Engineering
Fynjy0 [20]
3 years ago
8

If an atom gains an electron it is known as what ? And has a negative charge

Chemistry
1 answer:
bekas [8.4K]3 years ago
6 0
If an atom gains an electron and gets a negative charge because of it, it is a negatively charge ion AKA an anion.
You might be interested in
Which of the following is NOT a benefit of<br> using renewable energy sources?
Afina-wow [57]

Answer:

D, They produce fossil fuels

Explanation:

you can't just pull them out of nowhere

3 0
2 years ago
Read 2 more answers
ANSWER ASAP! PLEASE!
Eva8 [605]
Evaporation and straining.and idk the other two

4 0
3 years ago
Consider the elements bromine and chlorine; which element has a larger ionic radius
ipn [44]
Bromine has one more electron shell than the chlorine atom making the radius larger than the chlorine atom.
8 0
3 years ago
"At constant pressure, the volume of a fixed amount of gas is directly proportional to its absolute temperature." This is -
Lostsunrise [7]

Answer: B

Explanation:

According to Charle's law, at constant pressure the volume of a fixed mass of a ga is directly proportional to its absolute temperature.

At constant pressure, V∝T.

6 0
2 years ago
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids
VashaNatasha [74]

Answer:

The correct answer is: Serine, Histidine, Aspartate

Explanation:

The catalytic triad of an enzyme is composed of three aminoacid residues which are the most important for its catalytic activity. They are located in the catalytic site of the enzyme. In the case of chymotrypsin- a serine protease, the catalytic triad is composed by serine, histidine and aspartate (Ser-His-Asp). Serine proteases hydrolyse peptidic bonds in proteins and peptides. To do that, the histidine-which interacts with the aspartate by a hydrogen bond so its pKa increases- take a proton from the serine. Thus, deprotonated serine is able to attack the peptide bond and to perform hydrolysis.

8 0
3 years ago
Other questions:
  • PLEASE HELP<br> I really need someone to answer this!!!!
    11·2 answers
  • Daniel claims that the product of two square roots of integers is always rational. His reasoning is given in the example below.
    14·1 answer
  • Scoring: Your score will be based on the number of correct matches minus the number of incorrect matches. There is no penalty fo
    8·1 answer
  • The number of grams in the molar mass of an element is the same as an elements ...
    12·1 answer
  • Bleaching powder reaction, mechanism, use
    5·1 answer
  • Plate Tectonics Lab Report
    14·1 answer
  • 5. An example of a muscle that is voluntarily controlled is a muscle that
    11·1 answer
  • Definition of chemical change
    7·1 answer
  • What are the basic forces that drive the water cycle? Explain what they are.
    7·2 answers
  • Compare the type of change that occurs when a match is burnt and when a liquid starts boiling. Use complete sentences to justify
    15·1 answer
Add answer
Login
Not registered? Fast signup
Signup
Login Signup
Ask question!