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Literature DB >> 4362636

Prediction of secondary structure of proteins. A comparison of the phi, psi angles previously predicted for cytochrome c with recent x-ray crystallographic findings.

Abstract

Newer data from the x-ray crystallographic studies of tuna heart ferrocytochrome c have increased the number of residues in alpha-helical segments. This provided an objective test of our method of predicting varphi,Psi values for cytochrome c using the sequences of 18 cytochromes c and twenty 20 x 20 tables for the varphi,Psi values of tripeptides in 10 other proteins whose three-dimensional structures were known from x-ray crystallographic studies. Of the 32 residues now considered from x-ray data to be in alpha-helices, 27 had been predicted to be in the alpha-helical domain.

Entities: Chemical Species

Mesh：

Substances：
Cytochrome c Group

Year: 1974 PMID： 4362636 PMCID： PMC388123 DOI： 10.1073/pnas.71.3.899

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

Keyword Cloud
References

10 in total

1. An attempt to evaluate the influence of neighboring amino acids (n-1) and (n+1) on the backbone conformation of amino acid (n) in proteins. Use in predicting the three-dimensional structure of the polypeptide backbone of other proteins.

Authors: T T Wu; E A Kabat
Journal: J Mol Biol Date: 1973-03-25 Impact factor: 5.469

2. The structure of ferrocytochrome c at 2.45 A resolution.

Authors: T Takano; O B Kallai; R Swanson; R E Dickerson
Journal: J Biol Chem Date: 1973-08-10 Impact factor: 5.157

3. Construction of a three-dimensional model of the polypeptide backbone of the variable region of kappa immunoglobulin light chains.

Authors: E A Kabat; T T Wu
Journal: Proc Natl Acad Sci U S A Date: 1972-04 Impact factor: 11.205

4. The influence of nearest-neighbor amino acids on the conformation of the middle amino acid in proteins: comparison of predicted and experimental determination of -sheets in concanavalin A.

Authors: E A Kabat; T T Wu
Journal: Proc Natl Acad Sci U S A Date: 1973-05 Impact factor: 11.205

5. The influence of nearest-neighboring amino acid residues on aspects of secondary structure of proteins. Attempts to locate -helices and -sheets.

Authors: E A Kabat; T T Wu
Journal: Biopolymers Date: 1973-04 Impact factor: 2.505

10. An attempt to locate the non-helical and permissively helical sequences of proteins: application to the variable regions of immunoglobulin light and heavy chains.

Authors: T T Wu; E A Kabat
Journal: Proc Natl Acad Sci U S A Date: 1971-07 Impact factor: 11.205

10 in total

Prediction of secondary structure of proteins. A comparison of the phi, psi angles previously predicted for cytochrome c with recent x-ray crystallographic findings.

1. An attempt to evaluate the influence of neighboring amino acids (n-1) and (n+1) on the backbone conformation of amino acid (n) in proteins. Use in predicting the three-dimensional structure of the polypeptide backbone of other proteins.

2. The structure of ferrocytochrome c at 2.45 A resolution.

3. Construction of a three-dimensional model of the polypeptide backbone of the variable region of kappa immunoglobulin light chains.

4. The influence of nearest-neighbor amino acids on the conformation of the middle amino acid in proteins: comparison of predicted and experimental determination of -sheets in concanavalin A.

5. The influence of nearest-neighboring amino acid residues on aspects of secondary structure of proteins. Attempts to locate -helices and -sheets.

6. Model-building of neurohypophyseal hormones.

7. Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution.

8. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution.

9. Atomic co-ordinates for tosyl-alpha-chymotrypsin.

10. An attempt to locate the non-helical and permissively helical sequences of proteins: application to the variable regions of immunoglobulin light and heavy chains.