scholarly journals Protein conformational changes studied by diffusion NMR spectroscopy: Application to helix-loop-helix calcium binding proteins

2003 ◽  
Vol 12 (2) ◽  
pp. 228-236 ◽  
Author(s):  
A. M. Weljie
Keyword(s):  
Nmr Spectroscopy ◽  
Conformational Changes ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Helix Loop Helix ◽  
Diffusion Nmr ◽  
Protein Conformational Changes

scholarly journals Cation binding and conformational changes in VILIP and NCS-1, two neuron-specific calcium-binding proteins

1994 ◽  
Vol 269 (52) ◽  
pp. 32807-32813
Author(s):  
J A Cox ◽  
I Durussel ◽  
M Comte ◽  
S Nef ◽  
P Nef ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Cation Binding

Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments

1990 ◽  
Vol 68 (3) ◽  
pp. 587-601 ◽  
Author(s):  
Brian J. Marsden ◽  
Gary S. Shaw ◽  
Brian D. Sykes
Keyword(s):  
Binding Affinity ◽  
Sequence Homology ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Troponin C ◽  
Calcium Binding Proteins ◽  
Intact Protein ◽  
Peptide Fragments ◽  
Helix Loop Helix ◽  
Calcium Affinity

This paper describes the sequence homology of calcium-binding proteins belonging to the troponin C superfamily. Specifically, this similarity has been examined for 276 twelve-residue calcium-binding loops. It has been found that, in the calcium-binding loop, several residues appear invariant, regardless of the species of origin or the affinity of the protein. These residues are Asp at position 1 (+ X of the coordinating position of the calcium), Asp or Asn at position 3 (+ Y), Gly at position 6, Ile at position 8, and Glu at position 12 (− Z). It has also been found that conservation of certain residues can vary in similar sites in similar proteins. For example, position 3 (+ Y) in site 3 of troponin C is always an Asn, whereas in calmodulin the residue is always Asp. This study also examined the calcium-binding affinities of peptide fragments comprising the loop, helix–loop, loop–helix, and helix–loop–helix. These were compared with larger enzymatic or chemically generated protein fragments in an effort to understand the various contributions to the calcium-binding affinity of a single-site versus a two-site domain as found in troponin C and calmodulin. Based on free energy differences, it was found that a 34-residue helix–loop–helix peptide represents about 60% of the binding affinity found in the intact protein. Cooperativity with a second calcium binding site accounted for the remaining 40% of the affinity.Key words: calcium-binding proteins, sequence homology, peptide fragments, species variants, calcium affinity.

scholarly journals Design of Calcium-Binding Proteins to Sense Calcium

Molecules ◽  
2020 ◽  
Vol 25 (9) ◽  
pp. 2148 ◽  
Author(s):  
Shen Tang ◽  
Xiaonan Deng ◽  
Jie Jiang ◽  
Michael Kirberger ◽  
Jenny J. Yang
Keyword(s):  
Conformational Changes ◽  
Protein Design ◽  
Calcium Binding ◽  
Rational Design ◽  
Binding Proteins ◽  
Subsequent Development ◽  
Calcium Binding Proteins ◽  
Calcium Dependent ◽  
Calcium Sensors ◽  
Multiple Challenges

Calcium controls numerous biological processes by interacting with different classes of calcium binding proteins (CaBP’s), with different affinities, metal selectivities, kinetics, and calcium dependent conformational changes. Due to the diverse coordination chemistry of calcium, and complexity associated with protein folding and binding cooperativity, the rational design of CaBP’s was anticipated to present multiple challenges. In this paper we will first discuss applications of statistical analysis of calcium binding sites in proteins and subsequent development of algorithms to predict and identify calcium binding proteins. Next, we report efforts to identify key determinants for calcium binding affinity, cooperativity and calcium dependent conformational changes using grafting and protein design. Finally, we report recent advances in designing protein calcium sensors to capture calcium dynamics in various cellular environments.

How Important are S100A8/S100A9 Calcium Binding Proteins for the Activation of Phagocyte NADPH Oxidase, Nox2

2009 ◽  
Vol 8 (4) ◽  
pp. 282-289 ◽  
Author(s):  
Sylvie Berthier ◽  
Athan Baillet ◽  
Marie-Helene Paclet ◽  
Philippe Gaudin ◽  
Francoise Morel
Keyword(s):  
Nadph Oxidase ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Phagocyte Nadph Oxidase
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