On the relationship between the protein structure and protein dynamics

2008 ◽  
Vol 72 (2) ◽  
pp. 625-634 ◽  
Author(s):  
Chih-Hao Lu ◽  
Shao-Wei Huang ◽  
Yan-Long Lai ◽  
Chih-Peng Lin ◽  
Chien-Hua Shih ◽  
...  
Keyword(s):  
Protein Structure ◽  
Protein Dynamics ◽  
The Relationship

3. Proteins

2021 ◽  
pp. 34-51
Author(s):  
Mark Lorch
Keyword(s):  
Amino Acids ◽  
Protein Folding ◽  
Protein Structure ◽  
Protein Structures ◽  
Structure And Function ◽  
Vast Array ◽  
A Cell ◽  
Cellular Machinery ◽  
And Function ◽  
The Relationship

This chapter examines proteins, the dominant proportion of cellular machinery, and the relationship between protein structure and function. The multitude of biological processes needed to keep cells functioning are managed in the organism or cell by a massive cohort of proteins, together known as the proteome. The twenty amino acids that make up the bulk of proteins produce the vast array of protein structures. However, amino acids alone do not provide quite enough chemical variety to complete all of the biochemical activity of a cell, so the chapter also explores post-translation modifications. It finishes by looking as some dynamic aspects of proteins, including enzyme kinetics and the protein folding problem.

scholarly journals John Arthur Joseph Pateman. 18 May 1926—18 May 2011

2018 ◽  
Vol 65 ◽  
pp. 299-315
Author(s):  
Claudio Scazzocchio
Keyword(s):  
Gene Expression ◽  
Protein Structure ◽  
Genetic Information ◽  
Positive Control ◽  
Control Of Gene Expression ◽  
Academic Background ◽  
Eukaryotic Microorganisms ◽  
The Subject ◽  
Relationship Of ◽  
The Relationship

John Pateman was a distinguished British microbial geneticist. He came from a working-class area of London and a non-academic background. His earliest contribution to genetics was the discovery (together with John Fincham) of intracistronic complementation, an important phenomenon to understand the relationship of genetic information and protein structure; this at a time when the actual coding relationships of DNA and proteins were not yet worked out. Later on, he and his students made a fundamental contribution to the understanding of control of gene expression in eukaryotic microorganisms, providing some of the earliest examples of positive control. This work also led to the discovery of a new enzyme cofactor, the only one discovered through purely genetic evidence. He worked at various universities in Britain and Australia and trained a number of students who further developed the subject.

Nano-second protein dynamics of key residue at Position 38 in catechol-O-methyltransferase system: a time-resolved fluorescence study

2020 ◽  
Vol 168 (4) ◽  
pp. 417-425
Author(s):  
Fan Liu ◽  
Jianyu Zhang
Keyword(s):  
Protein Dynamics ◽  
Enzyme Catalysis ◽  
Time Resolved Fluorescence ◽  
Fluorescence Study ◽  
Time Resolved ◽  
System A ◽  
Key Enzyme ◽  
Relationship Of ◽  
The Relationship ◽  
Stokes Shifts

Abstract Human catechol-O-methyltransferase, a key enzyme related to neurotransmitter metabolism, catalyses a methyl transfer from S-adenosylmethionine to catechol. Although extensive studies aim to understand the enzyme mechanisms, the connection of protein dynamics and enzyme catalysis is still not clear. Here, W38in (Trp143Phe) and W38in/Y68A (Trp143Phe with Tyr68Ala) mutants were carried out to study the relationship of dynamics and catalysis in nano-second timescale using time-resolved fluorescence lifetimes and Stokes shifts in various solvents. The comprehensive data implied the mutant W38in/Y68A with lower activity is more rigid than the ‘WT’−W38in, suggesting the importance of flexibility at residue 38 to maintain the optimal catalysis.

Protein dynamics from NMR

1998 ◽  
Vol 76 (2-3) ◽  
pp. 145-152 ◽  
Author(s):  
Lewis E Kay
Keyword(s):  
Molecular Dynamics ◽  
Protein Structure ◽  
Protein Dynamics ◽  
Time Scales ◽  
Spin Relaxation ◽  
Biological Systems ◽  
Multidimensional Nmr ◽  
The Past ◽  
Wide Range ◽  
Nmr Methods

The past several years have seen the development of a significant number of new multidimensional NMR methods for the study of molecular dynamics spanning a wide range of time scales. Applications involving a large number of different biological systems have emerged and correlations with function have been established. Unique insights are obtained that are not available from structure alone, indicating the importance of dynamics studies for understanding function.Key words: NMR spin relaxation, protein dynamics, protein structure.

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