Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

Raj R.V. Dhanaraj; Jim E. Pitts; Phil Nugent; Poonsook Orprayoon; Jon B. Cooper; Tom L. Blundell; Jaana Uusitalo; Merja Penttilä

doi:10.1007/978-1-4615-1871-6_11

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

Raj R.V. Dhanaraj, Jim E. Pitts, Phil Nugent, Poonsook Orprayoon, Jon B. Cooper, Tom L. Blundell, Jaana Uusitalo, Merja Penttilä

Not published at Aalto University

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

Abstract

The protein engineering programme at Birkbeck seeks to develop generic methods based on a design cycle involving biochemical preparation and characterization, determination and comparative analysis of three-dimensional structures, rule-based design, site-directed mutagenesis and expression of the mutants. Knowledge of the tertiary structure of proteins and the use of molecular modelling techniques provide a powerful approach for the design of novel biomolecules with specifically engineered properties. The aspartic proteinase family have been studied in detail by X-ray analysis and provide a suitable data base for the development of protein engineering design principles1–6. This family of endopeptidases belonging to a wide range of biological species with varying substrate specificities. The members of the family are of considerable commercial importance since enzymes such as chymosin and Mucor pusillus pepsin have been exploited by the food industry in cheese and soya processing, while renins, cathepsins and the retroviral proteinases are prime targets of the pharmaceutical industries in drug design.

Original language	English
Title of host publication	Aspartic Proteinases
Editors	Kenji Takahashi
Publisher	Plenum Press
Pages	95-99
Number of pages	5
ISBN (Electronic)	978-1-4615-1871-6
ISBN (Print)	978-0-306-44830-0
DOIs	https://doi.org/10.1007/978-1-4615-1871-6_11
Publication status	Published - 1995
MoE publication type	A4 Conference publication
Event	International Conference on Aspartic Proteinases - Kawashimacho, Japan Duration: 19 Sept 1993 → 24 Sept 1993 Conference number: 5

Publication series

Name	Advances in Experimental Medicine and Biology
Publisher	Springer New York, NY
Volume	362
ISSN (Print)	0065-2598
ISSN (Electronic)	2214-8019

Conference

Conference	International Conference on Aspartic Proteinases
Country/Territory	Japan
City	Kawashimacho
Period	19/09/1993 → 24/09/1993

Access to Document

10.1007/978-1-4615-1871-6_11

Cite this

Dhanaraj, R. R. V., Pitts, J. E., Nugent, P., Orprayoon, P., Cooper, J. B., Blundell, T. L., Uusitalo, J., & Penttilä, M. (1995). Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. In K. Takahashi (Ed.), Aspartic Proteinases (pp. 95-99). (Advances in Experimental Medicine and Biology; Vol. 362). Plenum Press. https://doi.org/10.1007/978-1-4615-1871-6_11

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title = "Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant",

abstract = "The protein engineering programme at Birkbeck seeks to develop generic methods based on a design cycle involving biochemical preparation and characterization, determination and comparative analysis of three-dimensional structures, rule-based design, site-directed mutagenesis and expression of the mutants. Knowledge of the tertiary structure of proteins and the use of molecular modelling techniques provide a powerful approach for the design of novel biomolecules with specifically engineered properties. The aspartic proteinase family have been studied in detail by X-ray analysis and provide a suitable data base for the development of protein engineering design principles1–6. This family of endopeptidases belonging to a wide range of biological species with varying substrate specificities. The members of the family are of considerable commercial importance since enzymes such as chymosin and Mucor pusillus pepsin have been exploited by the food industry in cheese and soya processing, while renins, cathepsins and the retroviral proteinases are prime targets of the pharmaceutical industries in drug design.",

author = "Dhanaraj, {Raj R.V.} and Pitts, {Jim E.} and Phil Nugent and Poonsook Orprayoon and Cooper, {Jon B.} and Blundell, {Tom L.} and Jaana Uusitalo and Merja Penttil{\"a}",

year = "1995",

doi = "10.1007/978-1-4615-1871-6_11",

language = "English",

isbn = "978-0-306-44830-0",

series = "Advances in Experimental Medicine and Biology",

publisher = "Plenum Press",

pages = "95--99",

editor = "Kenji Takahashi",

booktitle = "Aspartic Proteinases",

address = "United States",

note = "International Conference on Aspartic Proteinases ; Conference date: 19-09-1993 Through 24-09-1993",

}

Dhanaraj, RRV, Pitts, JE, Nugent, P, Orprayoon, P, Cooper, JB, Blundell, TL, Uusitalo, J & Penttilä, M 1995, Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. in K Takahashi (ed.), Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol. 362, Plenum Press, pp. 95-99, International Conference on Aspartic Proteinases, Kawashimacho, Japan, 19/09/1993. https://doi.org/10.1007/978-1-4615-1871-6_11

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. / Dhanaraj, Raj R.V.; Pitts, Jim E.; Nugent, Phil et al.
Aspartic Proteinases. ed. / Kenji Takahashi. Plenum Press, 1995. p. 95-99 (Advances in Experimental Medicine and Biology; Vol. 362).

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

TY - GEN

T1 - Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

AU - Dhanaraj, Raj R.V.

AU - Pitts, Jim E.

AU - Nugent, Phil

AU - Orprayoon, Poonsook

AU - Cooper, Jon B.

AU - Blundell, Tom L.

AU - Uusitalo, Jaana

AU - Penttilä, Merja

N1 - Conference code: 5

PY - 1995

Y1 - 1995

N2 - The protein engineering programme at Birkbeck seeks to develop generic methods based on a design cycle involving biochemical preparation and characterization, determination and comparative analysis of three-dimensional structures, rule-based design, site-directed mutagenesis and expression of the mutants. Knowledge of the tertiary structure of proteins and the use of molecular modelling techniques provide a powerful approach for the design of novel biomolecules with specifically engineered properties. The aspartic proteinase family have been studied in detail by X-ray analysis and provide a suitable data base for the development of protein engineering design principles1–6. This family of endopeptidases belonging to a wide range of biological species with varying substrate specificities. The members of the family are of considerable commercial importance since enzymes such as chymosin and Mucor pusillus pepsin have been exploited by the food industry in cheese and soya processing, while renins, cathepsins and the retroviral proteinases are prime targets of the pharmaceutical industries in drug design.

AB - The protein engineering programme at Birkbeck seeks to develop generic methods based on a design cycle involving biochemical preparation and characterization, determination and comparative analysis of three-dimensional structures, rule-based design, site-directed mutagenesis and expression of the mutants. Knowledge of the tertiary structure of proteins and the use of molecular modelling techniques provide a powerful approach for the design of novel biomolecules with specifically engineered properties. The aspartic proteinase family have been studied in detail by X-ray analysis and provide a suitable data base for the development of protein engineering design principles1–6. This family of endopeptidases belonging to a wide range of biological species with varying substrate specificities. The members of the family are of considerable commercial importance since enzymes such as chymosin and Mucor pusillus pepsin have been exploited by the food industry in cheese and soya processing, while renins, cathepsins and the retroviral proteinases are prime targets of the pharmaceutical industries in drug design.

U2 - 10.1007/978-1-4615-1871-6_11

DO - 10.1007/978-1-4615-1871-6_11

M3 - Conference article in proceedings

SN - 978-0-306-44830-0

T3 - Advances in Experimental Medicine and Biology

SP - 95

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BT - Aspartic Proteinases

A2 - Takahashi, Kenji

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T2 - International Conference on Aspartic Proteinases

Y2 - 19 September 1993 through 24 September 1993

ER -

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

Abstract

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