K. Go

发表

Structure of 4-fluoro-1,3,5(10)-estratriene-3,17β-diol–hemimethanol

G. Kartha, K. Go, M. Neeman, 1982 .

The structure of ailanthol, a new triterpenoid from Ailanthus Malabarica DC

B. S. Joshi, S. Pelletier, K. Bhandary, 1985 .

Design of α-helical peptides: Their role in protein folding and molecular biology

R. Parthasarathy, K. Go, S. Chaturvedi, 1995 .

Crystal structure of (+)-isomenthyl p-bromophenylcarbamate and absolute configuration and conformation of isomenthol by X-ray diffraction and nuclear magnetic resonance studies

G. Kartha, A. Bose, M. Tibbetts, 1976 .

Crystal and molecular structure of 2-bromo-5,6-dihydro-6-methyl-4H,8H-pyrido [3,2,1-de]phenanthridin-8-one

G. Kartha, K. Nagarajan, K. Go, 1981 .

Crystal and molecular structure of 1-(p-bromobenzoyl)-2-methyl-1,2,3,4-tetrahydroquinoline

G. Kartha, K. Nagarajan, K. Go, 1977 .

Crystal structure and a twisted β‐sheet conformation of the tripeptide L‐leucyl‐L‐leucyl‐L‐leucine monohydrate trimethanol solvate: Conformation analysis of tripeptides

R. Parthasarathy, K. Go, 1995, Biopolymers.

The Structures of Four New C19-Diterpenoid Alkaloids from Aconitum forrestii Stapf

B. S. Joshi, J. Gliński, H. Chokshi, 1987 .

A sequence preference for nucleation of α‐helix—crystal structure of Gly‐L‐Ala‐L‐Val and Gly‐L‐Ala‐L‐Leu: Some comments on the geometry of leucine zippers

R. Parthasarathy, K. Go, S. Chaturvedi, 1991, Biopolymers.

Design of crystalline helices of short oligopeptides as a possible model for nucleation of alpha-helix: role of water molecules in stabilizing helices.

R. Parthasarathy, K. Go, S. Chaturvedi, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Structure of ouabagenin methanol solvate, C23H34O8.CH3OH

G. Kartha, K. Go, 1983 .

Structure of digoxin

J. P. Chen, G. Kartha, K. Go, 1980 .

Helix‐Forming tendencies of amino acids depend on their sequence contexts: Tripeptides AFG and FAG show incipient β‐bulge formation in their crystal structures

R. Parthasarathy, K. Go, S. Chaturvedi, 1993, Biopolymers.

Helix‐forming tendencies of amino acids depend on the restrictions of side‐chain rotamer conformations: Crystal structure of the tripeptide GAI in two crystalline forms

R. Parthasarathy, K. Go, S. Chaturvedi, 1992, Biopolymers.

The conformation of a constrained eight-membered ring.

I. Paul, K. Go, 1965 .