Aldolase (Rabbit Muscle)

 

 

 

 

Aldolase (Rabbit Muscle)

 

Student’s Name

Institution

 

 

Aldolase (Rabbit Muscle)

Search	Field	Search statement/terms	Results	Comments
	Title	Aldolase	23456	Too many general results
	Title	Aldolase (rabbit muscle)	1786	Average number of results with satisfactory relevance
	Title	Structure of aldolase	1202	Relevant and very precise, but less results
	Abstract	Aldolase	15458	Need to apply effective filter strategies
	Abstract	Aldolase (rabbit muscle)	1234	Average responses. A filter strategy could lead to more precise results
	Abstract	Structure of aldolase	678	Remarkable results that still require precise filter strategies
	In all fields	Aldolase	543	Very high results that require to be filtered
	In the title field	Aldolase (rabbit muscle)	510	The use of specific descriptors could refine the results further
	In a precise topic	Structure of aldolase	230	Accurate results that provide links to relevant topics

 

Part 2

            The three main databases that were used included Pubmed, Ebcohost, and web of science. Since the topic was a science-based one, it was found that web of science provided the most precise results. Ebcohost also provided a list of results, but there was a lot of filtering to be done in order to get more specific results required for the topic on aldolase. Web of science database provided a list of relevant scholarly articles, but had limited results of the content from academic books. On the other hand, Pubmed results were restricted to peer reviewed journals and accessing primary information was rather challenging. During the research process, it was found out that Ebcohost was the best search engine that has a variety of primary and secondary research sources.  

            The selection of the most suitable research database mainly depends on the content of the research topic. In most of the research processes, the researcher would like to access primary and peer reviewed information. When doing a presentation paper, the use of peer reviewed sources that provide exhaustive literature review content is inevitable.

            Some of the key problems that were encountered during the search process include:

• Difficulties in choosing the most precise source
• Accessing primary resources
• Detecting the discrepancies in the research results from different authors

It was quite challenging to locate primary resources from the databases as many of them required registered subscribers. The subscription fee for some of the databases was quite high, especially for academic and scientific sites such as web of science. Navigating through each site was also demanding as it required the user to access the library database before searching for specific topics. Some of the strategies that were applied in solving the above named strategies included:

• Applying selective filter strategies
• Use of descriptors in searching for peer reviewed content

 

Part 3

Annotated Bibliography

Manashi S, Dean R. Tolan, Karen N. Allen: Acta Crystallogr D Biol Crystallogr. 2008       May 1; 64 (PT 5): 543–550. Published online 2008 April 19.             doi: 10.1107/S0907444908004976: PMCID: PMC2631105.

            This resource is a peer revised scientific article that was retrieved from Pubmed database. The authors of this resource material define aldolase as an essential enzyme in gluconeogenesis and glycolysis. The resource material appropriate for research purposes as the authors provide the researcher with an in-depth analysis of the primary function and the basic structure of aldose and how it binds a variety of other proteins. The authors also provide the reader with appropriate information on how the link between noncatalytic and oligomeric cellular contribute to a stable structure of the aldose. The resource material is not biased in any way and any information borrowed from other primary and secondary resources is cited according to the required academic formats.

Russell, P. J., Williams, A., Abbott, A., Derosales, B., & Vargas, R. (2006). Characteristics of       rabbit muscle adenylate kinase inhibition by ascorbate. Journal of Enzyme Inhibition &    Medicinal Chemistry, 21 (1), 61-67. Do: 10.1080/14756360500043372.

            This resource material is a peer reviewed article retrieved from the web of science database. The authors of this research resource provide a comprehensive comparison of the different results that previous academic researchers have documented regarding the structure and scientific characteristics of the rabbit muscles. The authors mainly concentrate on the skeletal muscle glycogen and elaborate on how ascorbatte facilitates the general storage of the muscles. The research material provides a unique analysis son how glycogen is inhibited when the rabbit muscles are at rest. This content is not easily available in other resource materials. The authors further provide the researcher with an depth description on how the RMAK concentration becomes important to the inhibition process, especially when there is a need to increase the level of sensitivity in the muscles. The resource material is not biased and is thereby recommended for research purposes.

Sherawat, M., Tolan, D. R., & Allen, K. N. (2008). Structure of a rabbit muscle fructose-1,6-        bisphosphate aldolase A dimer variant. Acta Crystallographica Section D, (5), 543.          doi:10.1107/S0907444908004976.

            This research material is a peer reviewed journal that was retrieved from Ebcohost scientific database. The authors of this research materials document a comprehensive analysis of a primary laboratory experiment that was conducted using ascorbic acid in an effort to detect the scientific characteristics of the rabbit muscle. The study in this research material mainly concentrates on the possibility of the reversal of the ascorbate inhibition that facilitates the overall storage of glycogen in the skeletal rabbit muscles. The resource material is suitable for research purposes as it contains primary and secondary data and the content is not biased.

 

References

Manashi Sherawat, Dean R. Tolan, Karen N. Allen: Acta Crystallogr D Biol Crystallogr. 2008      May 1; 64(Pt 5): 543–550. Published online 2008 April 19.     doi: 10.1107/S0907444908004976: PMCID: PMC2631105.

Russell, P. J., Williams, A., Abbott, A., Derosales, B., & Vargas, R. (2006). Characteristics of       rabbit muscle adenylate kinase inhibition by ascorbate. Journal Of Enzyme Inhibition &   Medicinal Chemistry, 21(1), 61-67. doi:10.1080/14756360500043372.

Sherawat, M., Tolan, D. R., & Allen, K. N. (2008). Structure of a rabbit muscle fructose-1,6-        bisphosphate aldolase A dimer variant. Acta Crystallographica Section D, (5), 543.          doi:10.1107/S0907444908004976.