The three dimensional structures of proteins aid in delineating protein functions at a molecular level and the structure of proteins are determined usually with X ray crystallography, NMR spectroscopy etc. Some structural features of proteins would be necessary to perform certain biochemical functions although multifunctional and structural proteins may have higher number of residues than the average of 300 residues. Large aggregates are formed as a result of folding from protein subunits and actin molecules also assemble into actin filaments.
The protein structure has four distinct features including amino acid sequence of peptide chains as seen in a primary structure, secondary structures which are regular sub structures, such as strands of beta sheet, tertiary structure as seen in the three dimensional structure of a single protein molecule and quaternary structure which represents a complex of polypeptide chains and protein molecules (Copley, 1997; Berg, 2002). Proteins tend to transition between structures to perform the biological functions and this would be known as conformational changes.
The primary structure of proteins with amino acid sequences would be held together by covalent peptide bonds and the extremities of the amino acid chains are known as carboxy terminus (C - terminus) and amino terminus ( N -terminus).
The secondary structures are defined by their patterns of hydrogen bonds between the peptide groups although these bonds are generally not too stable except in conditions when the water concentration is low as in molten globule or fully folded states (Urbanc et al, 2006). The non specific interactions and propensities of amino acids would lead to the formation of molten globules. The tertiary structure shows structurally specific interactions within the protein domain with side chains and hydrogen bonds. The disulfide bonds tend to stabilize the tertiary structures of extra cellular proteins and reduce entropy in an unfolded state. The 4 levels of protein structure are given diagrammatically as follows -
Figure I - From Columbia.edu, biology courses, 2005 handouts
The formation of proteins could be explained as the combination of two amino acids in a condensation reaction and long chains of residues such as amino acids in peptide bond. The sequence of amino acids forms the primary structure of the peptide or protein and is determined by a gene. Within the primary structure, a sequence of nucleotides in DNA is transcribed into mRNA and this is translated by a ribosome and the sequence tends to define the structure and functions of the protein and would be unique to any specific protein. Determining the sequence of nucleotides within the primary structure would actually help in defining the protein (Berg, 2002; Copley, 1997). In the secondary structure, alpha helix and beta sheet saturate the peptide and secondary structures tend to occur most frequently in most proteins. The secondary structure elements tend to have a regular geometry with specific values and are usually folded into a shape with loops and turns (Berg, 2002, Copley, 1997). Tertiary structures are formed with interactions such as hydrogen bonding and ionic interactions and
This discussion is focused on the nature, structure and functions of proteins, how these are formed and the role played by folding and aggregation in protein and the various interactions that are part of protein functions.
Proteins are a class of macromolecules, also described as polymers of amino acids present in all biological organisms and made up of carbon, hydrogen, nitrogen and oxygen…
11 7. - Tools of the Trade; X-ray Crystallography and NMR. p.13 - Summary p. 16 References. p. 17 Abstract: A meta-analysis covering sixty years of biochemical research into the history and evolution of both the study and reality of proteins was conducted.
Resource allocation is one of the most important aspects of Construction Management. Resources are the true sources of the cost of the project. The management responsibilities lies with the proper utilization of available resources and at the same time to ensure that project delay does not occur due to resource constraints.
A Grid is a type of parallel and distributed system that enables the sharing, selection, and aggregation of resources distributed across 'multiple' administrative domains based on their (resources) availability, capacity, performance, cost and users' quality-of-service requirements"
You can fold or unfold them in 10 minutes. It is a unique and convenient vehicle, especially for short trips. Nowadays they are also used for entertainment in the park.
An advantage of folding bicycle is that, you can fold it up and put it into a bag. It is easy to carry with when you take bus or subway.
In many cases proteins may lose their tertiary and secondary structures through a process called denaturation, where the naturally occurring and functional native state of the protein is lost. Modern researchers have made numerous breakthroughs in the field
Examples of such diseases are degenerative diseases like Alzheimers disease, spongiform encephalopathies and Parkinsons disease. Infact, more than 40 different diseases related to protein deposition changes in the
Marketing communication manager has the responsibility of planning a consistent and integrated cross-team that has the sole responsibility of approaching these activities through his or her leadership. The team reinforces the company’s message to the target audience
The scooter itself weighs about 25kg just like a regular e-bike and is much easier since it does not need parking space (Monika. 2013). The scooter itself can be folded into halves without exposing or contaminating people with
This paper seeks to discuss some of the measures that can be taken into consideration when designing and producing product packages for a new product to be sold in the United States. In this particular case, the product and package will be produced in a small town in China and then shipped and sold in the United States.
These forces occur between side chains of individual amino acids to facilitate a stable structure.
Hydrophobic Interactions: These are weak interactions that occur when hydrophobic side chains of amino
3 pages (750 words)Essay
Hire a pro to write a paper under your requirements!
Win a special DISCOUNT!
Put in your e-mail and click the button with your lucky finger
Apply my DISCOUNT
Got a tricky question? Receive an answer from students like you!Try us!
Let us find you an essay for FREE
Contact us via Live Chat, call us at +16312120006or send an email to firstname.lastname@example.org