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The New Science Encyclopedia : Chemistry • Physics • Biology
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Plasma Science and Technology : Lectures in Physics, Chemistry, Biology, and Engineering
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Physics in Biology and Medicine
**Selected for Doody’s Core Titles® 2024 in Medical Physics** Physics in Biology and Medicine, Sixth Edition includes new, revised material, and corresponding exercises on many exciting developments in the field.New sections cover biomechanics, biotribology, frictional properties of biological materials, 3-D printing and its use in medicine, new materials in dentistry, microfluidics, bioelectronic medicine, microsensors, and microscopy.This revised edition delivers helpful and engaging additions to the role and importance of physics in biology and medicine, including new coverage on metamaterials, metabolism, and environmental science.It is ideal for courses in biophysics, medical physics, and related subjects.
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What are amino acids in chemistry?
Amino acids are organic compounds that serve as the building blocks of proteins. They contain an amino group (-NH2) and a carboxyl group (-COOH) attached to a central carbon atom, along with a side chain that is unique to each amino acid. There are 20 standard amino acids that are commonly found in proteins, each with different properties and functions. Amino acids play a crucial role in various biological processes, including enzyme function, cell signaling, and protein synthesis.
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What is the probability of amino acid frequency in biology?
The probability of amino acid frequency in biology refers to the likelihood of a specific amino acid occurring at a particular position in a protein sequence. This probability is influenced by various factors such as the genetic code, evolutionary conservation, and functional constraints. Different amino acids have different probabilities of occurring at specific positions, and this information is important for understanding protein structure, function, and evolution. By studying amino acid frequency, researchers can gain insights into the biological significance of specific protein sequences and make predictions about protein structure and function.
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What is the best natural science: Math, Physics, Biology, Chemistry, or Computer Science?
It is subjective to determine the "best" natural science as each field has its own unique contributions to our understanding of the natural world. Math provides the foundation for understanding and solving problems in all the other sciences. Physics explores the fundamental laws of nature and the behavior of matter and energy. Biology studies living organisms and their interactions with the environment. Chemistry focuses on the composition, structure, and properties of matter. Computer Science deals with the theory and practice of computation and information. Each of these sciences is valuable in its own right and contributes to our understanding of the world around us.
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What is the tertiary structure of amino acids in chemistry?
The tertiary structure of amino acids in chemistry refers to the three-dimensional arrangement of the atoms within a single protein molecule. This structure is determined by the interactions between the amino acid side chains, including hydrogen bonding, disulfide bridges, hydrophobic interactions, and electrostatic interactions. The tertiary structure is crucial for the function of proteins, as it determines their overall shape and the specific binding sites for other molecules. It is also important for the stability and activity of proteins.
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Physics in Biology and Medicine
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Why are amino acids divided into polar and nonpolar amino acids?
Amino acids are divided into polar and nonpolar categories based on the chemical properties of their side chains. This division is important because it helps to understand how amino acids interact with each other and with their environment. Polar amino acids have side chains that contain functional groups such as hydroxyl, amine, or carboxyl groups, which can form hydrogen bonds and interact with water. Nonpolar amino acids have side chains that are hydrophobic and do not readily interact with water. This classification is crucial for understanding protein structure, function, and interactions.
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Which subject should be removed: Chemistry, Biology, Physics, or Computer Science?
It is not advisable to remove any of these subjects as they all play a crucial role in providing a well-rounded education. Each subject offers unique perspectives and skills that are valuable for students' academic and professional development. Instead of removing a subject, it would be more beneficial to ensure that all students have access to a diverse range of subjects and resources to support their learning in each area.
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What is the chemical structure of the amino acids with an amino group (NH2) and a amino group (NH3)?
The chemical structure of amino acids with an amino group (NH2) and a carboxyl group (NH3) is characterized by a central carbon atom (alpha carbon) bonded to a hydrogen atom, an amino group (NH2), a carboxyl group (COOH), and a side chain (R group). The amino group (NH2) consists of a nitrogen atom bonded to two hydrogen atoms, while the carboxyl group (COOH) consists of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydroxyl group (OH). The side chain (R group) varies among different amino acids and determines their unique properties.
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What is the relationship between amino acids and pH in chemistry?
Amino acids are the building blocks of proteins and contain both acidic and basic functional groups. The pH of a solution can affect the charge of these functional groups, which in turn can affect the overall structure and function of the amino acid. At low pH, the carboxyl group of the amino acid is protonated and becomes positively charged, while the amino group remains unprotonated and neutral. At high pH, the carboxyl group is deprotonated and becomes negatively charged, while the amino group becomes protonated and positively charged. This pH-dependent charge on the functional groups of amino acids is important for their interactions with other molecules and their overall function in biological systems.
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